A parallel assembly of chromatography column modules connected in a rigid housing the assembly having one common assembly inlet and one common assembly outlet each column module comprising a bed space filled with chromatography medium and each column module comprises integrated fluid conduits which when the column module is connected with other column modules in the rigid housing are adapted to connect the bed space of the column module with the assembly inlet and the assembly outlet wherein the total length and/or volume of the fluid conduit from the assembly inlet to one bed space together with the length and/or volume of the fluid conduit from the same bed space to the assembly outlet is substantially the same for all bed spaces and modules installed in the parallel assembly.
B01D 15/22 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the construction of the column
B01D 15/18 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to flow patterns
F16L 55/00 - Devices or appurtenances for use in, or in connection with, pipes or pipe systems
G01N 30/46 - Flow patterns using more than one column
The present invention relates to a method for virus capture or separation. More closely, the invention relates to a method for direct influenza and adenovirus capture using magnetic beads. The method allows direct separation from crude cell lysate in a rapid manner.
The present disclosure is directed to a method for separating adeno-associated virus capsids fully packaged with genetic material from adeno-associated virus capsids not fully packaged with genetic material, the method comprising the following steps: a) adding a liquid sample comprising adeno-associated virus capsids to a chromatography material, wherein the liquid sample comprises adeno-associated virus capsids of a purity of at least 90% and of a concentration of at least 1012 adeno-associated virus capsids/ml, of which at least 10% of the adeno-associated virus capsids are adeno-associated virus capsids fully packaged with genetic material, wherein the chromatography material comprises a strong, or partially strong, anion exchange chromatography material comprising a support and a ligand for binding to the adeno-associated virus capsids; wherein the chromatography material comprises a surface extender connecting the ligand to the support, wherein the surface extender is a polymer, wherein the polymer is selected from: (i) a polymer having a naturally occurring skeleton, such as a polysaccharide, such as starch, cellulose, dextran, or agarose; and (ii) a polymer having a synthetic skeleton, such as a polyvinyl alcohol, a polyacrylamide, a polymethacrylamide, or a polyvinyl ether; b) eluting the adeno-associated virus capsids fully packaged with genetic material from the chromatography material; wherein the adeno-associated virus capsids eluted in step (b) are eluted into eluate fractions, which eluate fractions combined comprise at least 50% of the adeno-associated virus capsids of the liquid sample added in step (a), of which at least 60% of the adeno-associated virus capsids are fully packaged with genetic material. Further disclosed are compositions, including pharmaceutical compositions, obtained by said separation method, as well as uses of such compositions, and uses of an anion chromatography material for separation of adeno-associated virus capsids.
A linear precursor RNA molecule is provided, having a 5' end and a 3' end, and comprising in the 5'-to-3' direction i) a first self-splicing sequence, ii) a sequence of interest, and iii) a second self-splicing sequence, wherein the linear precursor RNA molecule is capable of forming a circular RNA upon splicing of said first and second self-splicing sequences; wherein the first self-splicing sequence comprises a first homopolymeric moiety located between said 5' end and a splice site first self-splicing sequence, and/or wherein the second self-splicing sequence comprises a second homopolymeric moiety located between said 3' end and a splice site of the second self-splicing sequence. The invention may improve the production and/or purification of circular RNA.
1211717222223322171733233217124124221717552332121222. The present disclosure also relates to a chromatography material comprising a support and the herein disclosed chromatography ligand coupled to the support, and a chromatography device comprising said chromatography material. Further disclosed is a use of said chromatography material or chromatography device for separating one or more target entities from impurities, as well as methods for separating one or more target entities from impurities.
B01J 20/289 - Phases chemically bonded to a substrate, e.g. to silica or to polymers bonded via a spacer
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
The present invention relates to protein purification, primarily in the chromatographic field. More closely, the invention relates to affinity chromatography using a split intein system comprising a C-intein tag and N-intein ligand, wherein the N-intein ligand provides increased solubility suitable for large scale purification of any recombinant target protein.
The disclosure relates to methods for purifying RNA from a sample using size exclusion chromatography (SEC). Uses of a SEC medium for purifying RNA from a sample are also provided.
The present disclosure relates to a class of engineered polypeptides having a binding affinity for the Fc region of immunoglobulins while exhibiting a significantly reduced binding affinity to the VH3 region of immunoglobulins. The present disclosure also relates to methods for isolating an immunoglobulin using said polypeptides as well as to related products, such as separation matrices.
C07K 14/31 - Peptides having more than 20 amino acidsGastrinsSomatostatinsMelanotropinsDerivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
C07K 1/22 - Affinity chromatography or related techniques based upon selective absorption processes
The present invention relates to porous cross-linked agarose gel beads which have a low agarose content, a method for the preparation of the beads and their use in chromatographic applications. The beads are suitable for the separation/purification of biomolecules from a biological sample. Due to the high porosity of the beads, they are especially suitable for separation/isolation of larger particles, such as virus particles e.g. adeno virus.
B01J 20/24 - Naturally occurring macromolecular compounds, e.g. humic acids or their derivatives
B01J 20/06 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof comprising inorganic material comprising oxides or hydroxides of metals not provided for in group
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
iii) a plurality of ligand groups covalently bound to the grafted polymer coating, wherein the ligand groups are capable of interacting with a target biomolecule.
B01D 15/32 - Bonded phase chromatography, e.g. with normal bonded phase, reversed phase or hydrophobic interaction
B01D 15/36 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction, e.g. ion-exchange, ion-pair, ion-suppression or ion-exclusion
The invention discloses method for manufacturing agar or agarose beads, comprising the steps of:
a) providing a water phase comprising an aqueous solution of agar or agarose at a temperature of 40-100° C.;
b) providing an oil phase comprising a water-immiscible solvent and an emulsifier at a temperature of 40-100° C.;
c) emulsifying the water phase in the oil phase to form a water-in-oil emulsion;
d) cooling the water-in-oil emulsion to a temperature below a gelation temperature of the agar or agarose to form a dispersion of solidified agar or agarose beads; and
e) recovering agar or agarose beads from the dispersion,
wherein the emulsifier comprises a phosphate ester of an alkoxylated fatty alcohol.
B01J 20/24 - Naturally occurring macromolecular compounds, e.g. humic acids or their derivatives
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
B01J 20/30 - Processes for preparing, regenerating or reactivating
The present invention provides a method (100) for separating a single-stranded nucleic acid molecule from one or more impurities, the method comprising: adding (110) a feed comprising the single-stranded nucleic acid molecule and one or more impurities to a chromatography medium comprising a matrix material functionalised with a hydrophobic ligand comprising an amine-derived aromatic group, and eluting (120) the single-stranded nucleic acid molecule from the chromatography medium. Further provided is the use of a chromatography medium for purification of a single-stranded nucleic acid molecule, wherein the chromatography medium comprises a matrix material functionalised with a hydrophobic ligand comprising an amine- derived aromatic group, as well as the use of a chromatography device for the purification of a single-stranded nucleic acid molecule, wherein the chromatography device comprises a chromatography medium for purification of a single-stranded nucleic acid molecule, wherein the chromatography medium comprises a matrix material functionalised with a hydrophobic ligand comprising an amine-derived aromatic group.
C12N 15/10 - Processes for the isolation, preparation or purification of DNA or RNA
B01D 15/32 - Bonded phase chromatography, e.g. with normal bonded phase, reversed phase or hydrophobic interaction
B01J 31/18 - Catalysts comprising hydrides, coordination complexes or organic compounds containing coordination complexes containing nitrogen, phosphorus, arsenic or antimony
C07D 213/04 - Heterocyclic compounds containing six-membered rings, not condensed with other rings, with one nitrogen atom as the only ring hetero atom and three or more double bonds between ring members or between ring members and non-ring members having three double bonds between ring members or between ring members and non-ring members having no bond between the ring nitrogen atom and a non-ring member or having only hydrogen or carbon atoms directly attached to the ring nitrogen atom
C07H 21/02 - Compounds containing two or more mononucleotide units having separate phosphate or polyphosphate groups linked by saccharide radicals of nucleoside groups, e.g. nucleic acids with ribosyl as saccharide radical
C12P 19/34 - Polynucleotides, e.g. nucleic acids, oligoribonucleotides
13.
ANTIBODY SEPARATION WITH A VH3 BINDING SEPARATION MATRIX
The present invention relates to processes of isolation of VH3 comprising antibodies or antibody fragments using a Protein A affinity separation matrix capable of binding VH3, wherein the elution buffer is a mono-, di- or tricarboxylic acid at a concentration of 50 mM or less. It further relates to a process for separation of bispecific antibodies or antibody fragments comprising one VH3 chain from antibodies or antibody fragments comprising two or more VH3 chain fragments.
The present disclosure is directed to a method for determining elution conditions suitable for separating adeno-associated virus (AAV) capsids fully packaged with genetic material from AAV capsids not fully packaged with genetic material, the method comprising: (a) adding a liquid sample comprising AAV capsids to a strong, or partially strong, anion exchange chromatography material comprising a surface extender, (b) eluting the AAV virus capsids from the chromatography material by applying an elution buffer comprising a step gradient of increasing conductivity, which increases by from about 0.5 to about 3 mS/cm per step, (c) based on an elution profile obtained in step (b), determining a first value of conductivity or conductivity-related parameter, which is suitable for eluting the adeno-associated virus capsids not fully packaged with genetic material, and (d) based on the elution profile obtained in step (b), determining a second value of conductivity or conductivity-related parameter, which is suitable for eluting the adeno-associated virus capsids fully packaged with genetic material. Further disclosed are methods for separating fully packaged AAV capsids from not fully packaged AAV capsids based on pre-determined first and second value of conductivity or conductivity-related parameter, as well as use of an anion exchange chromatography material for separating fully packaged AAV capsids from not fully packaged AAV capsids.
B01D 15/36 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction, e.g. ion-exchange, ion-pair, ion-suppression or ion-exclusion
B01D 15/42 - Selective adsorption, e.g. chromatography characterised by the development mode, e.g. by displacement or by elution
The present invention relates to a separation matrix for affinity chromatography and separation of biomolecules based on the presence of a kappa light chain. More specifically, the present invention relates to a separation matrix comprising at least 12 mg/ml kappa light chain-binding ligands covalently coupled to a porous support, wherein said kappa light chain-binding ligands comprise, consists essentially of, or consists of multimers of alkali-stabilized Finegoldia magna (formerly Peptostreptococcus magnus) Protein L domains; and wherein said porous support comprises polymer particles having a Dry solids weight (DW) of 50-200 mg/ml, a volume-weighted median diameter (D50v) of 30-100 μm. The invention also relates to methods of using said separation matrix.
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
C07K 1/22 - Affinity chromatography or related techniques based upon selective absorption processes
16.
A FUNCTIONALISED CHROMATOGRAPHY MEDIUM LACKING SURFACE EXTENDER
A chromatography medium is provided, comprising a matrix of cellulose-based nanofibers, the nanofibers optionally being crosslinked to one another. A ligand coupled to the matrix without any intermediate extender group. Also provided is a method of preparing a functionalised chromatography medium. The method comprises: (i) providing a substrate comprising cellulose acetate; (ii) forming a fibrous matrix/membrane spun of nanofibers from the substrate; (iii) saponification of the nanofibers to form regenerated cellulose nanofibers; (iv) derivatisation of the regenerated cellulose nanofibers with a cross-linker, and (v) coupling of a ligand to the derivatised cellulose nanofibers, wherein the preparation of the functionalised chromatography medium does not comprise any surface extender. The chromatography medium is useful for separation of large analytes, such as viruses.
B01J 20/289 - Phases chemically bonded to a substrate, e.g. to silica or to polymers bonded via a spacer
B01D 15/36 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction, e.g. ion-exchange, ion-pair, ion-suppression or ion-exclusion
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
B01J 20/24 - Naturally occurring macromolecular compounds, e.g. humic acids or their derivatives
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
C07K 16/18 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies against material from animals or humans
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
C07K 1/22 - Affinity chromatography or related techniques based upon selective absorption processes
C07K 16/08 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies against material from viruses
C07K 16/28 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
G01N 30/00 - Investigating or analysing materials by separation into components using adsorption, absorption or similar phenomena or using ion-exchange, e.g. chromatography
The invention provides an antigen-binding polypeptide capable of binding adeno-associated virus serotype 9 (AAV9), the polypeptide comprising a single-domain antibody (sdAb) variant having complementarity determining regions CDR1, CDR2 and CDR3 as disclosed herein. The antigen-binding polypeptide is useful as an affinity ligand for affinity capture applications, such as affinity separation.
A fusion protein comprising at least one first polypeptide moiety and at least one second polypeptide moiety, wherein the first polypeptide moiety is a single-chain polypeptide capable of binding a target entity, and the second polypeptide moiety is a stabilizing polypeptide and comprises a single-chain α-helix-containing domain, wherein the second polypeptide moiety does not have binding affinity for said target entity. The presence of the second polypeptide moiety can improve at least one property of the fusion protein as compared to the property of the first polypeptide moiety alone, wherein said improved property is selected from the group consisting of: alkaline stability, recombinant protein expression and coupling to a support.
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
C07K 14/31 - Peptides having more than 20 amino acidsGastrinsSomatostatinsMelanotropinsDerivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
C07K 16/00 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies
20.
A SUPPORT MATERIAL FOR SOLID-PHASE SYNTHESIS OF OLIGONUCLEOTIDES AND PEPTIDES
A cross-linked polysaccharide bead for use in a solid-phase support material for oligonucleotide sequence synthesis, peptide sequence synthesis, or oligonucleotide-peptide conjugate sequence synthesis is provided. The bead has at least one nucleoside, nucleotide or amino acid attached thereto, or has an entity attached thereto which entity is to form the basis for attachment of a first unit of a sequence to be synthesized.
C07H 21/00 - Compounds containing two or more mononucleotide units having separate phosphate or polyphosphate groups linked by saccharide radicals of nucleoside groups, e.g. nucleic acids
The present disclosure is directed to a method for separating supercoiled plasmid DNA (pDNA) from a liquid sample. the method comprising the steps of: (a) adding a liquid sample comprising pDNA to a first chromatography material comprising (i) an anion exchange chromatography ligand for binding to pDNA and (ii) a support material allowing convective flow through the first chromatography material, wherein the liquid sample originates from a cell culture harvest and has been subjected to a step of removing RNA before step (a): (b) eluting a liquid sample. comprising a purified mixture of supercoiled pDNA and open circular pDNA, from the first chromatography material: (c) adding the liquid sample from step (b) to a second chromatography material comprising a ligand that binds to pDNA and enables selective separation of supercoiled pDNA from open circular pDNA: (d) eluting the purified supercoiled pDNA from the second chromatography material: wherein the supercoiled pDNA eluted in step (d) has a purity degree of at least 95% without use of any further chromatography material than said first and second chromatography materials. Steps (a)-(d) and any intermediate steps can be completed within 5 hours. Further disclosed are uses of supercoiled pDNA obtained by said separation method.
The present disclosure is directed to a separation matrix comprising a plurality of chromatography particles, each chromatography particle comprising a core and a layer surrounding the core, wherein the core has a first average pore diameter and the layer surrounding the core has a second average pore diameter, wherein the second average pore diameter is at least 1.5 times higher than the first average pore diameter, wherein the first average pore diameter excludes diffusion of a target molecule through the pores of the core and wherein the second average pore diameter at least partly permits diffusion of the target molecule through the pores of the layer surrounding the core. Further disclosed are a method for preparing such a separation matrix, uses of such a separation matrix and methods for separating target molecules by use of such a separation matrix, in particular a method for separating adeno associated virus capsids fully packaged with genetic material from adeno associated virus capsids not fully packaged with genetic material, and compositions obtained by said method.
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
B01J 20/24 - Naturally occurring macromolecular compounds, e.g. humic acids or their derivatives
The present invention provides for a separation matrix for purification of antibodies or antibody fragments comprising at least one VH3 chain, said separation matrix comprising a VH3 binding ligand coupled to a porous support. Also provided is a method for isolation of antibodies or antibody fragments comprising at least one VH3 chain using the above-mentioned separation matrix. Additionally, there is provided a method for separation of bispecific antibodies or antibody fragments comprising one VH3 chain from variants of the antibody or antibody fragment comprising two VH3 chains or no VH3 chain, using the above-mentioned separation matrix.
C07K 14/31 - Peptides having more than 20 amino acidsGastrinsSomatostatinsMelanotropinsDerivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
C07K 16/06 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies from serum
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
C07K 1/22 - Affinity chromatography or related techniques based upon selective absorption processes
C07K 17/00 - Carrier-bound or immobilised peptidesPreparation thereof
The present invention relates to a method for virus purification. The present invention provides downstream processes for purification of adenovirus from cell culture harvest. More closely, it relates to a method for adenovirus purification using a virus capture and a virus polishing step.
The present disclosure is directed to a chromatography material comprising a support material functionalised with a ligand comprising a boronate moiety and use thereof for the separation of enveloped or membranous biological particles from impurities. Also disclosed are chromatography devices and a method for separating enveloped or membranous biological particles from impurities, comprising adding a liquid sample comprising enveloped or membranous biological particles and one or more impurities, to a chromatography material comprising a support material functionalised with a ligand comprising a boronate moiety, and eluting the enveloped or membranous biological particles from the chromatography material in at least one eluate fraction using an elution buffer, the elution buffer optionally comprising a poly-hydroxyl compound, such as sucrose or sorbitol.
B01J 20/289 - Phases chemically bonded to a substrate, e.g. to silica or to polymers bonded via a spacer
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
A method for packing a chromatography column with chromatography media, comprising the steps of: providing a system comprising a column tube having a closed first end comprising an inlet/outlet, a media inlet adjacent a second end of the column tube and an adaptor positioned inside the column tube initially adjacent the second end of the column tube for sliding and sealing contact with an inner face of the column tube, the column tube and adaptor arranged initially such that they define an internal volume and such that the media inlet is in fluid connection with the internal volume; connecting a media slurry source to the media inlet; at least partially filling the internal volume with media slurry via the media inlet; forcing the adaptor towards the first end of the column tube to reduce the internal volume such that the media inlet is no longer in fluid connection with the reduced internal volume.
B01D 15/20 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the conditioning of the sorbent material
B01D 15/22 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the construction of the column
The present relates to a polypeptide that binds to an immunoglobulin or a fragment thereof. More specifically, it relates to a kappa light-chain binding polypeptide with high binding affinity and improved alkali stability. The one kappa light-chain binding comprises a mutated binding domain of Peptostreptococcus Protein L, derived from any one of the amino acid sequences SEQ ID NO:10, SEQ ID NO:11, SEQ ID NO:12, SEQ ID NO:13, SEQ ID NO:14, SEQ ID NO:15, SEQ ID NO:16, SEQ ID NO:17 or SEQ ID NO:18, said amino acid sequences having N6H, N41H and N56Y or N56Q mutations.
Disclosed herein is a protein for affinity capture, the protein comprising: a ligand moiety capable of affinity interaction with a target molecule, and a linker moiety bound to the ligand moiety and capable of being coupled to a solid phase, wherein the ligand moiety is free from lysine residues, and wherein the linker moiety is terminally positioned in the protein and has at least two lysine residues, wherein at least one residue other than lysine is terminally arranged in relation to at least two of the lysine residues. Further disclosed is an affinity capture medium comprising the protein, a split intein system for affinity capture of a protein of interest, and a method for purification of a protein of interest.
A method of purifying extracellular vesicles or enveloped viruses is provided. The method comprises obtaining a solution volume comprising extracellular vesicles or enveloped viruses and contaminants, adding the solution volume to a size exclusion chromatography column comprising a stationary phase comprising a packed bed of cross-linked polysaccharide beads, and collecting an eluate volume comprising the extracellular vesicles or enveloped viruses exiting the column. Advantageously, the method is scalable and can be used in large scale or industrial scale processes.
The present disclosure is directed to a chromatography system comprising a buffer valve arrangement configured to allow independent control of a first buffer feed and a second buffer feed; a pump arrangement configured to supply a first buffer feed, a second buffer feed, and a feed comprising a biological target compound and one or more impurities; a selection valve arrangement, comprising a first chromatography device selection valve; a first chromatography device, comprising a first chromatography material comprising a support material functionalised with a ligand, wherein the ligand comprises an anion exchange group or an affinity group having a binding affinity for a biological target compound; a second chromatography device, comprising a second chromatography material, which comprises a conditioning chromatography material; wherein the selection valve arrangement is configured to enable separation of a biological target compound from impurities by allowing a feed, comprising a biological target compound and one or more impurities, to continuously pass through the first chromatography device and the second chromatography device, wherein the first chromatography device and the second chromatography device are configured to be connected in series. The disclosure also provides use of the chromatography system and a method for separation of enveloped or membranous biological particles from one or more impurities.
B01D 15/18 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to flow patterns
B01D 15/20 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the conditioning of the sorbent material
B01D 15/34 - Size-selective separation, e.g. size-exclusion chromatographyGel filtrationPermeation
B01D 15/36 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction, e.g. ion-exchange, ion-pair, ion-suppression or ion-exclusion
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
C12N 7/00 - Viruses, e.g. bacteriophagesCompositions thereofPreparation or purification thereof
31.
A CHROMATOGRAPHY MATERIAL, USE THEREOF, AND A METHOD FOR SEPARATING ADENO-ASSOCIATED CAPSIDS
The present disclosure is directed to a chromatography material comprising a support material in the form of a convection-based membranous structure comprising nanofibres, wherein the support material is functionalised with an anion exchange ligand at a ligand density of <300 µmol/mL, wherein the chromatography material comprises a linker connecting the ligand to the support material, the linker comprising a linear backbone having a length of 2-16 atoms. Also provided is a chromatography device comprising a holder comprising the chromatography material as disclosed herein. Additionally, the present disclosure is directed to use of the herein disclosed chromatography material or chromatography device for separating adeno-associated virus capsids fully packaged with genetic material from adeno-associated virus capsids not fully packaged with genetic material. Further, the present disclosure provides a method for separating adeno-associated virus capsids fully packaged with genetic material from adeno-associated virus capsids not fully packaged with genetic material, the method comprising the following steps: (a) adding a liquid sample comprising adeno-associated virus capsids to the chromatography material as disclosed herein, wherein the liquid sample comprises adeno-associated virus capsids of a purity of at least 90% and of a concentration of at least 1012 adeno-associated virus capsids/ml, of which at least 10% of the adeno-associated virus capsids are adeno-associated virus capsids fully packaged with genetic material; (b) eluting the adeno-associated virus capsids fully packaged with genetic material from the chromatography material; wherein the adeno-associated virus capsids eluted in step (b) are eluted into at least one eluate fraction, which eluate fraction comprises at least 50% of the fully packaged adeno-associated virus capsids present in the liquid sample added in step (a), and wherein at least 60% of the adeno-associated virus capsids eluted in step (b) are fully packaged with genetic material.
B01D 15/36 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction, e.g. ion-exchange, ion-pair, ion-suppression or ion-exclusion
B01D 15/12 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the preparation of the feed
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
The present disclosure is directed to a chromatography system comprising a buffer valve arrangement configured to allow independent control of a first buffer feed and a second buffer feed; a pump arrangement configured to supply a first buffer feed, a second buffer feed, and a feed comprising a biological target compound and one or more impurities; a selection valve arrangement, comprising a first chromatography device selection valve; a first chromatography device comprising a first chromatography material comprising a support material functionalised with a ligand, wherein the ligand comprises an affinity group having a binding affinity for a biological target compound, an ion exchange group, or a multimodal group; a second chromatography device, comprising a second chromatography material, which comprises a conditioning chromatography material; a third chromatography device comprising a third chromatography material; wherein the selection valve arrangement is configured to enable separation of biological target compounds from impurities by allowing a feed, comprising biological target molecules and one or more impurities, to continuously pass through the first, the second, and the third chromatography devices, wherein the first, the second, and the third chromatography devices are configured to be connected in series. Further provided are a use of the chromatography system and a method for separation of adeno-associated virus capsids from one or more impurities.
B01D 15/18 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to flow patterns
B01D 15/36 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction, e.g. ion-exchange, ion-pair, ion-suppression or ion-exclusion
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
C12N 7/00 - Viruses, e.g. bacteriophagesCompositions thereofPreparation or purification thereof
A chromatography medium for separating an analyte in a solution is provided, the chromatography medium comprising a matrix material having a mean flow pore size of 0.1- 2.0 µm, wherein the matrix material is functionalized with a thiophilic aromatic ligand to a ligand concentration up to 1500 µmol/g matrix material. Provided are also processes of separating an analyte in a solution using the chromatography medium. The invention is useful for separating different isoforms of plasmid DNA.
Method of clarifying a crude protein solution, the method comprising to provide (100) a volume of the crude protein solution, mixing (101) Na2HPO4 and CaCl2) in water, forming a first solution, adding (102) the first solution to the volume of crude protein solution, thereby forming a second solution. NaCl is added to the first solution, the crude protein solution and/or to the second solution. The second solution is mixed (103). The thus formed flocculated material is separated (104) from the second solution, obtaining a clarified protein solution. The clarified protein solution may thereafter be purified by chromatography.
The present invention relates to a method of purifying an antibody or an antibody fragment, adsorbing at least one of the antibody or the antibody fragment onto an affinity separation matrix by contacting a liquid sample with the affinity separation matrix; wherein the affinity matrix is an affinity separation matrix comprises a ligand based on Protein L, or any variation thereof that binds to a κ-light chain of the antibody or antibody fragment, and separating the at least one antibody or antibody fragment from the affinity separation matrix by using an elution buffer, wherein the elution buffer has concentration of 5-50 mM. It equally relates to a method for separation of bispecific antibodies.
An anion exchange chromatography medium (1) for use in purification of enveloped virus particles or exosomes from a feed, the anion exchange chromatography medium comprising a support material being functionalized with a ligand comprising a diamine functionality generating at least one weak anion exchange group to an ionic capacity of 10-500 μmol/mL.
B01D 15/36 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction, e.g. ion-exchange, ion-pair, ion-suppression or ion-exclusion
B01J 41/20 - Anion exchangers for chromatographic processes
The present invention relates to a method of separating bispecific antibodies or bispecific antibody fragments. The method comprises the steps of a) providing a feed comprising bispecific antibodies or bispecific antibody fragments; b) contacting the feed with a separation matrix having affinity ligands coupled to a support; c) optionally washing the separation resin with a washing liquid; d) applying an elution buffer to the separation resin, to elute the antibodies or antibody fragments bound to the affinity ligand; wherein in step d) a pH gradient is applied over the elution buffer, said pH gradient being from about 6 to about 2.
The invention discloses a method for cleaning or sanitization of an affinity chromatography matrix, comprising the steps of:
The invention discloses a method for cleaning or sanitization of an affinity chromatography matrix, comprising the steps of:
a) providing an affinity chromatography matrix having oxidation-tolerant proteinaceous ligands coupled to a support,
The invention discloses a method for cleaning or sanitization of an affinity chromatography matrix, comprising the steps of:
a) providing an affinity chromatography matrix having oxidation-tolerant proteinaceous ligands coupled to a support,
b) contacting the matrix with a sanitization solution comprising at least one oxidant defined by formula I,
The invention discloses a method for cleaning or sanitization of an affinity chromatography matrix, comprising the steps of:
a) providing an affinity chromatography matrix having oxidation-tolerant proteinaceous ligands coupled to a support,
b) contacting the matrix with a sanitization solution comprising at least one oxidant defined by formula I,
The invention discloses a method for cleaning or sanitization of an affinity chromatography matrix, comprising the steps of:
a) providing an affinity chromatography matrix having oxidation-tolerant proteinaceous ligands coupled to a support,
b) contacting the matrix with a sanitization solution comprising at least one oxidant defined by formula I,
wherein R is hydrogen or an acyl group R′—C(O)—, with R′ being a hydrogen or a methyl, ethyl or propyl group.
B01D 15/20 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the conditioning of the sorbent material
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
G01N 30/50 - Conditioning of the sorbent material or stationary liquid
39.
Parallel Assembly of Chromatography Column Modules
A parallel assembly of chromatography column modules, the assembly having one common assembly inlet and one common assembly outlet, each column module comprising a bed space filled with chromatography medium and each column module comprises integrated fluid conduits which when the column module is connected with other column modules are adapted to connect the bed space of the column module with the assembly inlet and the assembly outlet, wherein the total length and/or volume of the fluid conduit from the assembly inlet to one bed space together with the length and/or volume of the fluid conduit from the same bed space to the assembly outlet is substantially the same for all bed spaces and modules installed in the parallel assembly.
B01D 15/14 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the introduction of the feed to the apparatus
B01D 15/18 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to flow patterns
B01D 15/22 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the construction of the column
G01N 30/46 - Flow patterns using more than one column
A chromatography medium comprising porous beads having an inner porous core and an outer porous shell is used for chromatographic separation of enveloped or membranous biological particles from impurities such as contaminant DNA and/or protein. The core is capable of binding molecules via hydrophobic interactions; however, the pore size of the shell does not allow particles having a size of 20 nm and larger to permeate into the bead and interact with the core. The separation is performed at a pH of less than 7.4. The enveloped or membranous biological particles may have been subjected to a prior chromatographic capture step. When used for purification of enveloped virus particles the inventive process was found to yield a remarkably high rate of infectious virus particles.
B01D 15/32 - Bonded phase chromatography, e.g. with normal bonded phase, reversed phase or hydrophobic interaction
B01D 15/34 - Size-selective separation, e.g. size-exclusion chromatographyGel filtrationPermeation
B01D 15/36 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction, e.g. ion-exchange, ion-pair, ion-suppression or ion-exclusion
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
B01D 15/16 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the conditioning of the fluid carrier
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
A chromatography system for at least one of tangential flow chromatography and lateral flow chromatography comprising: an inlet; a functionalised adsorbent chromatography medium downstream of the inlet; an outlet downstream of the adsorbent chromatography medium; and a flow guide downstream of the inlet and upstream of the adsorbent chromatography medium and configured to distribute a flow of a liquid from the inlet across a width of the adsorbent chromatography medium; wherein the flow guide comprises a pattern of channels providing flow paths from the inlet to different parts of the adsorbent chromatography medium along the width of the adsorbent chromatography medium, wherein the pattern of channels is provided so as to reduce a difference in arrival time and/or flow velocity of liquid reaching the adsorbent chromatography medium across the width of the adsorbent chromatography medium.
The present invention relates to a method for purifying a feed comprising a concentration of a target product in a chromatography system (10) having a first adsorption purifying unit (13). The first adsorption purifying unit has a capacity for binding the target product and is configured to receive the feed from a first holding tank (12), receiving continuous feed from a bioreactor (11), and to provide the target product (14) at an outlet (13b). The method comprises: a) loading (S20) the first adsorption purifying unit (13) with a volume of feed provided from the first holding tank (12), the volume of feed comprising an amount of the at least one target product corresponding to less than, or equal to, the capacity for binding the target product in the first adsorption purifying unit, b) washing, eluting, cleaning and regenerating (S30) the first adsorption purifying unit (13) while filling the first holding tank (12) with feed, said first holding tank (12) having a volume of at least the amount of the feed provided by the bioreactor (11) during this step, and repeating step a) and b) for a predetermined number of cycles.
B01D 15/18 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to flow patterns
B01D 15/20 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the conditioning of the sorbent material
C12M 1/00 - Apparatus for enzymology or microbiology
43.
A CHROMATOGRAPHY DEVICE, SYSTEM, AND USE THEREOF FOR ANALYTIC SEPARATION
1233 are independently selected from C1-C3 alkyl, CH2OH, and CH2CHOHCH3, wherein the volume of the chromatography material is from about 0.1 mL to about 2 mL. Further disclosed are uses of said chromatography device and a method for separating adeno-associated virus capsids fully packaged with genetic material from adeno- associated virus capsids not fully packaged with genetic material, as well as a kit of parts and a chromatography system for use in analytic separation of adeno-associated capsids.
The present invention relates to protein purification, primarily in the chromatographic field. More closely, the invention relates to affinity chromatography using a split intein system with an improved C-intein tag and N-intein ligand, wherein the target protein may be purified as a tag-less end product with a native N-terminus.
The present invention relates to a method for controlling fraction collection of a target product 27 in a chromatography system 49 configured for cyclic purification performed on a sample comprising the target product 27. The method comprises determining trigger points for target product 27 collection in relation to presence of target product in the outlet; setting a first time period based on the trigger points within which the elution in the first cycle is captured; evaluating timing of the captured elution to identify the next time period; applying the timing to capture elution during the elution phase in the following cycle; and collecting the captured elution in the following cycle. The last three steps are repeated to capture the elution during the elution phase of the following cycles until no more target product 27 is desired.
B01D 15/24 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the treatment of the fractions to be distributed
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
B01D 15/42 - Selective adsorption, e.g. chromatography characterised by the development mode, e.g. by displacement or by elution
12151-31-32152221512151215311 is CO. The present disclosure also relates to a chromatography material comprising a support and the herein disclosed chromatography ligand coupled to the support. Further disclosed is a use of said chromatography material for separating one or more target molecules from impurities, as well as a method for separating one or more target molecules from impurities.
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
B01D 15/36 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction, e.g. ion-exchange, ion-pair, ion-suppression or ion-exclusion
B01D 15/42 - Selective adsorption, e.g. chromatography characterised by the development mode, e.g. by displacement or by elution
B01J 20/289 - Phases chemically bonded to a substrate, e.g. to silica or to polymers bonded via a spacer
The invention relates to processes for purification of poly-tagged products, such as mRNA, from synthetic or biological compositions. The process involves contacting the composition with a oligo d (T)-functionalized chromatography medium comprising a convection-based chromatography material.
C12N 15/10 - Processes for the isolation, preparation or purification of DNA or RNA
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
B01J 20/289 - Phases chemically bonded to a substrate, e.g. to silica or to polymers bonded via a spacer
48.
A PROCESS AND CHROMATOGRAPHY MATERIAL FOR CHROMATOGRAPHY RECOVERY OF NUCLEIC ACID MOLECULES
The present disclosure relates to a process for recovery of a nucleic acid product from a composition. The process (100) comprising: (i) contacting (110) the composition with a chromatography material functionalised with a ligand. The chromatography material comprises nanofibers; (ii) optionally washing (120) the functionalised chromatography material with a washing liquid phase; (iii) selectively eluting (130) said product by contacting the functionalised chromatography material with an elution liquid phase; (iv) cleaning-in-place (140) comprising regenerating the chromatography material by contacting with a cleaning liquid phase; (v) repeating steps (i)-(iii) for at least 15 cycles, wherein step (iv) is performed in at least one of said cycles; and (vi) collecting (150) recovered nucleic acid product. The chromatography material being capable of retaining a dynamic binding capacity at 10% breakthrough for said product after 50 cycles that is at least 80% of the corresponding dynamic binding capacity of the first cycle.
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
C07K 1/16 - ExtractionSeparationPurification by chromatography
C12N 15/10 - Processes for the isolation, preparation or purification of DNA or RNA
B01D 15/20 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the conditioning of the sorbent material
49.
Method of Cleaning and/or Sanitizing a Separation Matrix
The present invention concerns a method of cleaning and/or sanitizing a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains covalently coupled to a porous support. The method comprises the steps of:
a) optionally purifying a mixture comprising a first immunoglobulin using the separation matrix;
b) providing a cleaning liquid comprising at least 50% by volume of an aqueous alkali metal hydroxide solution; and
c) cleaning and/or sanitizing the separation matrix by contacting the cleaning liquid with the separation matrix for a predetermined contact time.
The present invention concerns a method of cleaning and/or sanitizing a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains covalently coupled to a porous support. The method comprises the steps of:
a) optionally purifying a mixture comprising a first immunoglobulin using the separation matrix;
b) providing a cleaning liquid comprising at least 50% by volume of an aqueous alkali metal hydroxide solution; and
c) cleaning and/or sanitizing the separation matrix by contacting the cleaning liquid with the separation matrix for a predetermined contact time.
The alkali-stabilized Protein A domains comprise mutants of a parental Fc-binding domain of Staphylococcus Protein A (SpA), as defined by SEQ ID NO 51 or SEQ ID NO 52, wherein the amino acid residues at positions 13 and 44 of SEQ ID NO 51 or 52 are asparagines and wherein at least the asparagine residue at position 3 of SEQ ID NO 51 or 52 has been mutated to an amino acid selected from the group consisting of glutamic acid, lysine, tyrosine, threonine, phenylalanine, leucine, isoleucine, tryptophan, methionine, valine, alanine, histidine and arginine.
C07K 14/31 - Peptides having more than 20 amino acidsGastrinsSomatostatinsMelanotropinsDerivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
C07K 16/00 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies
C07K 16/12 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies against material from bacteria
C07K 17/10 - Peptides being immobilised on, or in, an organic carrier the carrier being a carbohydrate
C07K 16/06 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies from serum
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
B01J 20/286 - Phases chemically bonded to a substrate, e.g. to silica or to polymers
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
C07K 14/31 - Peptides having more than 20 amino acidsGastrinsSomatostatinsMelanotropinsDerivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
51.
A PRE-SCREENING METHOD AND A METHOD FOR SEPARATING ADENO-ASSOCIATED VIRUS CAPSIDS
The present disclosure is directed to a method for determining elution conditions suitable for separating adeno-associated virus (AAV) capsids fully packaged with genetic material from AAV capsids not fully packaged with genetic material, the method comprising: (a) adding a liquid sample comprising AAV capsids to a strong, or partially strong, anion exchange chromatography material comprising a surface extender, (b) eluting the AAV virus capsids from the chromatography material by applying an elution buffer comprising a step gradient of increasing conductivity, which increases by from about 0.5 to about 3 mS/cm per step, (c) based on an elution profile obtained in step (b), determining a first value of conductivity or conductivity-related parameter, which is suitable for eluting the adeno-associated virus capsids not fully packaged with genetic material, and (d) based on the elution profile obtained in step (b), determining a second value of conductivity or conductivity-related parameter, which is suitable for eluting the adeno-associated virus capsids fully packaged with genetic material. Further disclosed are methods for separating fully packaged AAV capsids from not fully packaged AAV capsids based on pre-determined first and second value of conductivity or conductivity-related parameter, as well as use of an anion exchange chromatography material for separating fully packaged AAV capsids from not fully packaged AAV capsids.
Staphylococcus protein A (SpA), or a functional fragment or variant thereof. The chromatography ligand presents an advantageous capability of withstanding harsh cleaning in place (CIP) conditions, and is capable of binding Fab fragments of antibodies. The ligand may be provided with a terminal coupling group, such as arginine or cysteine, to facilitate its coupling to an insoluble carrier such as beads or a membrane. The invention also relates to a process of using the ligand in isolation of antibodies, and to a purification protocol which may include washing steps and/or regeneration with alkali.
B01J 20/24 - Naturally occurring macromolecular compounds, e.g. humic acids or their derivatives
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
C07K 1/22 - Affinity chromatography or related techniques based upon selective absorption processes
C07K 14/31 - Peptides having more than 20 amino acidsGastrinsSomatostatinsMelanotropinsDerivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
C07K 16/00 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies
C07K 17/00 - Carrier-bound or immobilised peptidesPreparation thereof
C07K 17/10 - Peptides being immobilised on, or in, an organic carrier the carrier being a carbohydrate
An Fc-binding polypeptide of improved alkali stability, comprising a mutant of an Fc-binding domain of Staphylococcus Protein A (SpA), as defined by SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO:3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:22, SEQ ID NO 51 or SEQ ID NO 52 wherein at least the asparagine or serine residue at the position corresponding to position 11 in SEQ ID NO:4-7 has been mutated to an amino acid selected from the group consisting of glutamic acid, lysine, tyrosine, threonine, phenylalanine, leucine, isoleucine, tryptophan, methionine, valine, alanine, histidine and arginine.
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
C07K 16/06 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies from serum
C07K 1/22 - Affinity chromatography or related techniques based upon selective absorption processes
C07K 14/31 - Peptides having more than 20 amino acidsGastrinsSomatostatinsMelanotropinsDerivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
C07K 16/00 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies
Finegoldia magna (formerly Peptostreptococcus Magnus)WW) of 50-200 mg/ml, a volume-weighted median diameter (D50v) of 30-100 μm. The invention also relates to methods of using said separation matrix.
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
The present disclosure relates to a class of engineered polypeptides having a binding affinity for the VH3 region of immunoglobulins and exhibiting desirable alkali clean stability properties. Additionally, the polypeptides exhibit significantly reduced binding affinity for the Fc region of immunoglobulins. The present disclosure also relates to methods for isolating an immunoglobulin or fragment thereof using said polypeptides as well as to related products.
C07K 14/31 - Peptides having more than 20 amino acidsGastrinsSomatostatinsMelanotropinsDerivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
b) the porous support comprises cross-linked polymer particles having a volume-weighted median diameter (d50,v) of 56-70 micrometers and a dry solids weight of 55-80 mg/ml.
C07K 1/22 - Affinity chromatography or related techniques based upon selective absorption processes
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
B01J 20/24 - Naturally occurring macromolecular compounds, e.g. humic acids or their derivatives
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
B01J 20/286 - Phases chemically bonded to a substrate, e.g. to silica or to polymers
C07K 14/31 - Peptides having more than 20 amino acidsGastrinsSomatostatinsMelanotropinsDerivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
C07K 16/00 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies
C07K 16/06 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies from serum
C07K 17/10 - Peptides being immobilised on, or in, an organic carrier the carrier being a carbohydrate
The present disclosure is directed to a method for separating supercoiled plasmid DNA (pDNA) from a liquid sample, the method comprising the steps of: (a) adding a liquid sample comprising pDNA to a first chromatography material comprising (i) an anion exchange chromatography ligand for binding to pDNA and (ii) a support material allowing convective flow through the first chromatography material, wherein the liquid sample originates from a cell culture harvest and has been subjected to a step of removing RNA before step (a); (b) eluting a liquid sample, comprising a purified mixture of supercoiled pDNA and open circular pDNA, from the first chromatography material; (c) adding the liquid sample from step (b) to a second chromatography material comprising a ligand that binds to pDNA and enables selective separation of supercoiled pDNA from open circular pDNA; (d) eluting the purified supercoiled pDNA from the second chromatography material; wherein the supercoiled pDNA eluted in step (d) has a purity degree of at least 95% without use of any further chromatography material than said first and second chromatography materials. Steps (a)-(d) and any intermediate steps can be completed within 5 hours. Further disclosed are uses of supercoiled pDNA obtained by said separation method.
C12N 15/10 - Processes for the isolation, preparation or purification of DNA or RNA
B01D 15/36 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction, e.g. ion-exchange, ion-pair, ion-suppression or ion-exclusion
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
C07K 1/22 - Affinity chromatography or related techniques based upon selective absorption processes
58.
A FUNCTIONALISED CHROMATOGRAPHY MEDIUM LACKING SURFACE EXTENDER
A chromatography medium is provided, comprising a matrix of cellulose-based nanofibers, the nanofibers optionally being crosslinked to one another. A ligand coupled to the matrix without any intermediate extender group. Also provided is a method of preparing a functionalised chromatography medium. The method comprises: (i) providing a substrate comprising cellulose acetate; (ii) forming a fibrous matrix/membrane spun of nanofibers from the substrate; (iii) saponification of the nanofibers to form regenerated cellulose nanofibers; (iv) derivatisation of the regenerated cellulose nanofibers with a cross-linker, and (v) coupling of a ligand to the derivatised cellulose nanofibers, wherein the preparation of the functionalised chromatography medium does not comprise any surface extender. The chromatography medium is useful for separation of large analytes, such as viruses.
B01J 20/24 - Naturally occurring macromolecular compounds, e.g. humic acids or their derivatives
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
C07K 14/31 - Peptides having more than 20 amino acidsGastrinsSomatostatinsMelanotropinsDerivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
C07K 16/06 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies from serum
C07K 16/12 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies against material from bacteria
C07K 17/10 - Peptides being immobilised on, or in, an organic carrier the carrier being a carbohydrate
The invention discloses a separation matrix comprising a plurality of multimodal ligands covalently coupled to a support, wherein said support is a membrane comprising nonwoven polymer fibers and wherein said ligands are capable of interacting with a target biomacromolecule. Further, the invention discloses separation methods using the separation matrix.
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
B01D 69/02 - Semi-permeable membranes for separation processes or apparatus characterised by their form, structure or propertiesManufacturing processes specially adapted therefor characterised by their properties
The present disclosure is directed to a separation matrix comprising a plurality of chromatography particles, each chromatography particle comprising a core and a layer surrounding the core, wherein the core has a first average pore diameter and the layer surrounding the core has a second average pore diameter, wherein the second average pore diameter is at least 1.5 times higher than the first average pore diameter, wherein the first average pore diameter excludes diffusion of a target molecule through the pores of the core and wherein the second average pore diameter at least partly permits diffusion of the target molecule through the pores of the layer surrounding the core. Further disclosed are a method for preparing such a separation matrix, uses of such a separation matrix and methods for separating target molecules by use of such a separation matrix, in particular a method for separating adeno associated virus capsids fully packaged with genetic material from adeno associated virus capsids not fully packaged with genetic material, and compositions obtained by said method.
B01D 15/32 - Bonded phase chromatography, e.g. with normal bonded phase, reversed phase or hydrophobic interaction
B01D 15/36 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction, e.g. ion-exchange, ion-pair, ion-suppression or ion-exclusion
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
B01J 20/286 - Phases chemically bonded to a substrate, e.g. to silica or to polymers
B01J 20/289 - Phases chemically bonded to a substrate, e.g. to silica or to polymers bonded via a spacer
The present invention relates to a preparative chromatography system (200, 500, 800) and a chromatography process (400, 700) adapted to repetitive cycling of chromatography volumes. The system (200, 500, 800) comprises at least two upstream pumps (203a, 803a, 203b, 803b) and separate flow paths (220) from process liquid sources to the chromatography device (200, 500, 800). The system (200, 500, 800) is arranged to prime one flow path (220) with one process liquid while providing another process liquid to the chromatography device and thereby minimizing the hold-up volume of the system (200, 500, 800).
B01D 15/18 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to flow patterns
B01D 15/20 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the conditioning of the sorbent material
B01D 15/42 - Selective adsorption, e.g. chromatography characterised by the development mode, e.g. by displacement or by elution
B01D 15/24 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the treatment of the fractions to be distributed
A chromatography device (201; 201′) comprising: – at least one chromatography material unit (203), wherein said chromatography material unit comprises a convection-based chromatography material and is of a substantially rectangular shape having a length (L) and a width (W); - at least one fluid distribution system (207) which is configured to distribute fluid into and out from the at least one chromatography material unit (203), wherein said fluid distribution system (207) comprises a distribution device (209a) and a collection device (209b) between which said chromatography material unit (203) is sandwiched, wherein said distribution device (209a) and said collection device (209b) each comprises a number of parallel grooves (255) for distribution and collection respectively of a fluid to be passed through the chromatography material unit (203), wherein said parallel grooves are reaching over substantially the whole length (L) of the chromatography material unit (203) and are distributed over substantially the whole width (W) of the chromatography material unit (203).
B01D 15/14 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the introduction of the feed to the apparatus
B01D 15/22 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the construction of the column
B01D 15/18 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to flow patterns
B01D 15/26 - Selective adsorption, e.g. chromatography characterised by the separation mechanism
The invention discloses a method of distinguishing empty and full capsids in a virus preparation or loaded and non-loaded non-viral gene therapy vectors. The method comprises the steps of: a) providing a preparation of viral particles or gene therapy vectors; b) subjecting the preparation to interferometric scattering mass spectrometry (ISCAMS), in an interferometric scattering microscope, to generate mass distribution data for the viral particles; c) determining the levels of empty capsids and capsids comprising a genome among the viral particles or the loaded and non-loaded vectors from the mass distribution data.
A parallel assembly of chromatography column modules connected in a rigid housing the assembly having one common assembly inlet and one common assembly outlet each column module comprising a bed space filled with chromatography medium and each column module comprises integrated fluid conduits which when the column module is connected with other column modules in the rigid housing are adapted to connect the bed space of the column module with the assembly inlet and the assembly outlet wherein the total length and/or volume of the fluid conduit from the assembly inlet to one bed space together with the length and/or volume of the fluid conduit from the same bed space to the assembly outlet is substantially the same for all bed spaces and modules installed in the parallel assembly.
B01D 15/22 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the construction of the column
B01D 15/18 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to flow patterns
F16L 55/00 - Devices or appurtenances for use in, or in connection with, pipes or pipe systems
G01N 30/46 - Flow patterns using more than one column
The present disclosure relates to a class of engineered polypeptides having a binding affinity for the Fc region of immunoglobulins while exhibiting a significantly reduced binding affinity to the VH3 region of immunoglobulins. The present disclosure also relates to methods for isolating an immunoglobulin using said polypeptides as well as to related products, such as separation matrices.
C07K 16/06 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies from serum
C07K 16/32 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies against material from animals or humans against translation products from oncogenes
C07K 14/31 - Peptides having more than 20 amino acidsGastrinsSomatostatinsMelanotropinsDerivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
C07K 1/16 - ExtractionSeparationPurification by chromatography
C07K 1/22 - Affinity chromatography or related techniques based upon selective absorption processes
C07K 16/00 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies
67.
Chromatographic methods for purification of proteins from plasma
The present invention relates to the field of chromatography. More closely, the invention relates to a chromatographic method for purification of proteins, such as Factor VIII, von Willebrand factor and Factor IX. The chromatographic method is performed on a matrix comprising an inner porous core and outer porous lid surrounding said core.
B01J 41/20 - Anion exchangers for chromatographic processes
B01D 15/36 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction, e.g. ion-exchange, ion-pair, ion-suppression or ion-exclusion
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
A61K 38/36 - Blood coagulation or fibrinolysis factors
A61K 38/48 - Hydrolases (3) acting on peptide bonds (3.4)
C12N 9/64 - Proteinases derived from animal tissue, e.g. rennin
B01D 15/34 - Size-selective separation, e.g. size-exclusion chromatographyGel filtrationPermeation
C07K 14/47 - Peptides having more than 20 amino acidsGastrinsSomatostatinsMelanotropinsDerivatives thereof from animalsPeptides having more than 20 amino acidsGastrinsSomatostatinsMelanotropinsDerivatives thereof from humans from vertebrates from mammals
The present relates to a polypeptide that binds to an immunoglobulin or a fragment thereof. More specifically, it relates to a kappa light-chain binding polypeptide with high binding affinity and improved alkali stability. The one kappa light-chain binding comprises a mutated binding domain of Peptostreptococcus Protein L, derived from any one of the amino acid sequences SEQ ID NO:10, SEQ ID NO:11, SEQ ID NO:12, SEQ ID NO:13, SEQ ID NO:14, SEQ ID NO:15, SEQ ID NO:16, SEQ ID NO:17 or SEQ ID NO:18, said amino acid sequences having N6H, N41H and N56Y or N56Q mutations.
A parallel assembly of chromatography column modules, the assembly having one common assembly inlet and one common assembly outlet, each column module comprising a bed space filled with chromatography medium and each column module comprises integrated fluid conduits which when the column module is connected with other column modules are adapted to connect the bed space of the column module with the assembly inlet and the assembly outlet, wherein the total length and/or volume of the fluid conduit from the assembly inlet to one bed space together with the length and/or volume of the fluid conduit from the same bed space to the assembly outlet is substantially the same for all bed spaces and modules installed in the parallel assembly.
B01D 15/14 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the introduction of the feed to the apparatus
B01D 15/18 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to flow patterns
B01D 15/22 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the construction of the column
G01N 30/46 - Flow patterns using more than one column
The present disclosure is directed to a method for separating adeno-associated virus capsids fully packaged with genetic material from adeno-associated virus capsids not fully packaged with genetic material, the method comprising the following steps: a) adding a liquid sample comprising adeno-associated virus capsids to a chromatography material, wherein the liquid sample comprises adeno-associated virus capsids of a purity of at least 90% and of a concentration of at least 1012 adeno-associated virus capsids/ml, of which at least 10% of the adeno-associated virus capsids are adeno-associated virus capsids fully packaged with genetic material, wherein the chromatography material comprises a strong, or partially strong, anion exchange chromatography material comprising a support and a ligand for binding to the adeno-associated virus capsids; wherein the chromatography material comprises a surface extender connecting the ligand to the support, wherein the surface extender is a polymer, wherein the polymer is selected from: (i) a polymer having a naturally occurring skeleton, such as a polysaccharide, such as starch, cellulose, dextran, or agarose; and (ii) a polymer having a synthetic skeleton, such as a polyvinyl alcohol, a polyacrylamide, a polymethacrylamide, or a polyvinyl ether; b) eluting the adeno-associated virus capsids fully packaged with genetic material from the chromatography material; wherein the adeno-associated virus capsids eluted in step (b) are eluted into eluate fractions, which eluate fractions combined comprise at least 50% of the adeno-associated virus capsids of the liquid sample added in step (a), of which at least 60% of the adeno-associated virus capsids are fully packaged with genetic material. Further disclosed are compositions, including pharmaceutical compositions, obtained by said separation method, as well as uses of such compositions, and uses of an anion chromatography material for separation of adeno-associated virus capsids.
The present invention relates to a method for virus capture or separation. More closely, the invention relates to a method for direct influenza and adenovirus capture using magnetic beads. The method allows direct separation from crude cell lysate in a rapid manner.
The present invention relates to a method of separating bispecific antibodies or bispecific antibody fragments. The method comprises the steps of a) providing a feed comprising bispecific antibodies or bispecific antibody fragments; b) contacting the feed with a separation matrix having affinity ligands coupled to a support; c) optionally washing the separation resin with a washing liquid; d) applying an elution buffer to the separation resin, to elute the antibodies or antibody fragments bound to the affinity ligand; wherein in step d) a pH gradient is applied over the elution buffer, said pH gradient being from about 6 to about 2.
C07K 1/00 - General processes for the preparation of peptides
C07K 1/22 - Affinity chromatography or related techniques based upon selective absorption processes
C07K 16/36 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies against material from animals or humans against blood coagulation factors
C07K 16/32 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies against material from animals or humans against translation products from oncogenes
C07K 16/06 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies from serum
73.
CHROMATOGRAPHY MEDIUM FOR USE IN PURIFICATION OF ENVELOPED VIRUS PARTICLES OR EXOSOMES
An anion exchange chromatography medium (1) for use in purification of enveloped virus particles or exosomes from a feed, the anion exchange chromatography medium comprising a support material being functionalized with a ligand comprising a diamine functionality generating at least one weak anion exchange group to an ionic capacity of 10-500 µmol/mL.
B01J 20/24 - Naturally occurring macromolecular compounds, e.g. humic acids or their derivatives
B01D 15/36 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction, e.g. ion-exchange, ion-pair, ion-suppression or ion-exclusion
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
01 - Chemical and biological materials for industrial, scientific and agricultural use
Goods & Services
Assay for detecting, analyzing and quantifying affinity ligand in the purification process using chemical reagents for industrial, research and laboratory purposes
A separation matrix comprising porous particles to which antibody-binding protein ligands have been covalently immobilized, wherein the density of said ligands is above 5 mg/ml, the volume-weighted median diameter of said porous particles is at least 10 and below 30 μm and the said porous particles have a gel phase distribution coefficient, expressed as KD for dextran of molecular weight 110 kDa, of 0.5-0.9.
B01J 20/286 - Phases chemically bonded to a substrate, e.g. to silica or to polymers
B01D 15/18 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to flow patterns
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
The present invention relates to protein purification, primarily in the chromatographic field. More closely, the invention relates to affinity chromatography using a split intein system comprising a C-intein tag and N-intein ligand, wherein the N-intein ligand provides increased solubility suitable for large scale purification of any recombinant target protein.
2422 in water, forming a first solution, adding (102) the first solution to the volume of crude protein solution, thereby forming a second solution. NaCl is added to the first solution, the crude protein solution and/or to the second solution. The second solution is mixed (103). The thus formed flocculated material is separated (104) from the second solution, obtaining a clarified protein solution. The clarified protein solution may thereafter be purified by chromatography.
The invention discloses a method for separation of antibodies or antibody fragments, comprising the steps of: a) providing a feed comprising antibodies or antibody fragments having a VH3 region and being devoid of an Fc region capable of binding to Protein A; b) contacting the feed with a separation resin having covalently coupled ligands, wherein the ligands comprise a polypeptide as defined by SEQ ID NO 1 and wherein the antibodies or antibody fragments bind to the separation resin; c) optionally washing the separation resin with a washing liquid; d) eluting the antibodies or antibody fragments from the separation resin with an elution liquid and recovering the antibodies or antibody fragments.
A chromatography device (1; 101) comprising: —at least one chromatography material unit (3), wherein said chromatography material unit comprises a convection-based chromatography material; —at least one fluid distribution system (7) which is configured to distribute fluid into and out from the at least one chromatography material unit (3); —an inlet (15); —at least one inlet fluid channel (17a, 17b) connecting the inlet (15) with each chromatography material unit (3) via the fluid distribution system (7); —an outlet (19); and —at least one outlet fluid channel (21) connecting the outlet (19) with each chromatography material unit (3) via the fluid distribution system (7), wherein at least some parts of said chromatography device (1; 101) are overmolded and sealed together by plastic or elastomer leaving at least the inlet (15) and the outlet (19) open.
B01D 15/22 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the construction of the column
B01D 15/26 - Selective adsorption, e.g. chromatography characterised by the separation mechanism
B01D 15/18 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to flow patterns
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
A chromatography system for at least one of tangential flow chromatography and lateral flow chromatography comprising: an inlet; a functionalised adsorbent chromatography medium downstream of the inlet; an outlet downstream of the adsorbent chromatography medium; and a flow guide downstream of the inlet and upstream of the adsorbent chromatography medium and configured to distribute a flow of a liquid from the inlet across a width of the adsorbent chromatography medium; wherein the flow guide comprises a pattern of channels providing flow paths from the inlet to different parts of the adsorbent chromatography medium along the width of the adsorbent chromatography medium, wherein the pattern of channels is provided so as to reduce a difference in arrival time and/or flow velocity of liquid reaching the adsorbent chromatography medium across the width of the adsorbent chromatography medium.
The present invention is within the field of chromatography. More precisely, it relates to a novel chromatography medium, namely a hydrophobic medium provided with different lids excluding molecules over a certain size due to the porosity of the hydrophobic medium and/or the porosity of the lid. The invention also relates to use of the separation medium for purification of large molecules, which do not enter the separation medium, as well as small molecules, which enter the separation medium and are eluted from there.
B01J 39/26 - Cation exchangers for chromatographic processes
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
The present invention relates to a novel chromatography media, more closely a novel IMAC (Immobilized Metal Affinity Chromatography) media. The novel chromatography media comprises a pentaligand and provides high dynamic binding capacity as well as high purity of the sample proteins purified on the media of the invention.
B01J 20/289 - Phases chemically bonded to a substrate, e.g. to silica or to polymers bonded via a spacer
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
The invention relates to processes for purification of poly-tagged products, such as mRNA, from synthetic or biological compositions. The process involves contacting the composition with a oligo d (T)-functionalized chromatography medium comprising a convection-based chromatography material.
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
B01J 20/286 - Phases chemically bonded to a substrate, e.g. to silica or to polymers
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
C07H 1/08 - SeparationPurification from natural products
C12N 15/10 - Processes for the isolation, preparation or purification of DNA or RNA
The invention discloses method for manufacturing agar or agarose beads, comprising the steps of: a) providing a water phase comprising an aqueous solution of agar or agarose at a temperature of 40-100° C.: b) providing an oil phase comprising a water-immiscible solvent and an emulsifier at a temperature of 40-100° C.; c) emulsifying the water phase in the oil phase to form a water-in-oil emulsion: d) cooling the water-in-oil emulsion to a temperature below a gelation temperature of the agar or agarose to form a dispersion of solidified agar or agarose beads: and e) recovering agar or agarose beads from dispersion, wherein the emulsifier comprises a phosphate ester of an alkoxylated fatty alcohol.
B01J 20/24 - Naturally occurring macromolecular compounds, e.g. humic acids or their derivatives
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
The present invention relates to a method for purification of plasma proteins. More closely, the invention relates to a method using magnetic beads for separation of different plasma proteins from a plasma fraction, such as a cryoprecipitate or cryosupernatant of plasma, or alternatively directly from cell culture of recombinant plasma proteins.
A chromatography system comprising at least two chromatography units (3) connected in parallel, wherein said at least two chromatography units (3) each comprises a convection-based chromatography material, wherein an initial difference in back pressure provided from the different chromatography units (3) is compensated dynamically during run of the system due to a change of chromatography unit properties provided during the chromatography process.
B01D 15/18 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to flow patterns
B01D 15/14 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the introduction of the feed to the apparatus
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
B01D 15/36 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction, e.g. ion-exchange, ion-pair, ion-suppression or ion-exclusion
B01J 20/286 - Phases chemically bonded to a substrate, e.g. to silica or to polymers
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
B01J 41/20 - Anion exchangers for chromatographic processes
B01J 47/127 - Ion-exchange processes in generalApparatus therefor characterised by the use of ion-exchange material in the form of ribbons, filaments, fibres or sheets, e.g. membranes in the form of filaments or fibres
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
C07K 1/22 - Affinity chromatography or related techniques based upon selective absorption processes
C07K 14/31 - Peptides having more than 20 amino acidsGastrinsSomatostatinsMelanotropinsDerivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
C07K 16/06 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies from serum
The invention discloses a separation matrix comprised of porous spherical particles to which antibody-binding protein ligands have been covalently immobilized, wherein the density of said ligands is in the range of 10.5-15 mg/ml and the volume-weighted median diameter of said particles is in the range of 30-55 μm.
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
B01J 20/24 - Naturally occurring macromolecular compounds, e.g. humic acids or their derivatives
B01J 20/286 - Phases chemically bonded to a substrate, e.g. to silica or to polymers
C07K 1/22 - Affinity chromatography or related techniques based upon selective absorption processes
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
C07K 16/06 - Immunoglobulins, e.g. monoclonal or polyclonal antibodies from serum
The invention discloses a method of manufacturing polysaccharide beads, comprising the steps of: i) providing a water phase comprising an aqueous solution of a polysaccharide; ii) providing an oil phase comprising at least one water-immiscible organic solvent and at least one oil-soluble emulsifier; iii) emulsifying the water phase in the oil phase to form a water-in-oil (w/o) emulsion; and iv) inducing solidification of the water phase in the w/o emulsion, wherein the organic solvent is an aliphatic or alicyclic ketone or ether.
The present invention relates to porous cross-linked agarose gel beads which have a low agarose content, a method for the preparation of the beads and their use in chromatographic applications. The beads are suitable for the separation/purification of biomolecules from a biological sample. Due to the high porosity of the beads, they are especially suitable for separation/isolation of larger particles, such as virus particles e.g. adeno virus.
B01J 20/24 - Naturally occurring macromolecular compounds, e.g. humic acids or their derivatives
B01J 20/06 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof comprising inorganic material comprising oxides or hydroxides of metals not provided for in group
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
A separation system may include a number of parallel fluid paths. Each parallel fluid path may include a separation module, and an adjustable flow restrictor. Each adjustable flow restrictor is operable sequentially and operable such that the hydraulic resistance of all the parallel fluid paths is substantially the same and is equal to or higher than the hydraulic resistance of a fluid path identified to have the highest hydraulic resistance. The system includes a pressure sensor that measures pressure loss over the whole separation system. The system is operable such that the hydraulic resistances of the respective separation modules are synchronised, and such that when operated in parallel and at substantially the same time, the respective modules have substantially the same time residence times. The system may include a control system for automated operation.
Functionalised polymeric chromatography medium, comprising: at least one non-woven sheet comprising one or more polymeric nanofibers having a mean diameter of 10-1000 nm; one or more polymer chains grafted onto the one or more polymeric nanofibers, wherein the polymer chains are poly-glycerol chains comprising glycidol monomer residues or wherein the polymer chains comprise divinylsulfone monomer residues; and at least one ligand group bonded to the one or more polymer chains.
B01D 15/20 - Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the conditioning of the sorbent material
B01D 15/38 - Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups , e.g. affinity, ligand exchange or chiral chromatography
B01J 20/28 - Solid sorbent compositions or filter aid compositionsSorbents for chromatographyProcesses for preparing, regenerating or reactivating thereof characterised by their form or physical properties
B01J 20/286 - Phases chemically bonded to a substrate, e.g. to silica or to polymers
B01J 20/289 - Phases chemically bonded to a substrate, e.g. to silica or to polymers bonded via a spacer
B01J 20/30 - Processes for preparing, regenerating or reactivating
The present invention relates to a method for virus purification. The present invention provides downstream processes for purification of adenovirus from cell culture harvest. More closely, it relates to a method for adenovirus purification using a virus capture and a virus polishing step.
