Abstract: An antibody-resin coupling apparatus quickly and efficiently activates resin beads and couples them to antibodies, while preventing breakdown and crosslinking of the beads, thereby improving downstream column purification processes, extending the usable life of the resin beads, and increasing molecule capture efficiency of the resultant resin-antibody complexes, to allow improved isolation and purification of factor VIII molecules or other drug compounds.

Abstract: The present invention relates to a method for purifying anti-IL-6 receptor antibodies from a sample comprising said antibodies and impurities, through the use of a three-chromatographic columns procedure, including a chromatography on Fluorapatite-containing resin. The invention is also concerned with pharmaceutical compositions comprising the purified antibodies obtainable by the process of the invention.

Abstract: Chromatography resins having anionic exchange-hydrophobic mixed mode ligands and methods of using such resins are provided.

Abstract: The present invention relates to a biologic that inhibits angiogenesis. In particular, the present invention relates to fusion proteins that inhibit the integrin activated pathway and one other angiogenic factor-activated pathway as well as formulation compositions of such fusion proteins, as well as methods for producing and using the same.

Abstract: 1) A method for obtaining a concentrated protein-rich phase from residues of bioethanol production. 2.1) Previously, the separation of a protein-rich phase from whole stillage from bioethanol production has been achieved either by the addition of chemicals or by process steps that are complex in terms of equipment and/or energy. 2.2) Whole stillage from bioethanol production is fed to a solid-liquid separation, and the liquid phase (thin stillage) resulting from this is partially returned to the mashing process. This recirculation increases the raw protein content in the process. Part of the thin stillage is diluted and fed to a simple separation process without the addition of chemicals and temperature treatment, with a protein-rich phase being obtained. 2.3) A protein-rich phase is obtained from residues of bioethanol production.

Abstract: Provided are self-crosslinking meditope-enabled antibodies. Also provided are methods for altering the distribution of a cell surface antigen using self-crosslinking meditope enabled antibodies, compositions for use in the methods, and methods of producing, using, testing, and screening the same, including therapeutic and diagnostic methods and uses.

Abstract: Provided herein is an aptamer specific to coagulation factor XIII (FXIII) and its uses thereof. Accordingly, the present aptamer is useful as a bio-tool to label thrombi, and/or as a targeting molecule to deliver drugs to thrombotic area. Therefore, the present disclosure also pertains to methods for treating diseases associated with FXIII, such as thrombosis.

Abstract: Processes and methods of purifying or separating Single Domain Antigen Binding (SDAB) molecules that include one or more single binding domains (e.g., one or more nanobody molecules), substantially devoid of a complementary antibody domain and an immunoglobulin constant region, using Protein A-based affinity chromatography, are disclosed.

Abstract: The invention relates to a method for providing a drug delivery system, in particular for crossing the blood brain barrier (BBB), comprising a virus-like particle (VLP) derived from John Cunningham virus (JCV), a drug delivery system and novel VLP obtainable by said method. The method comprises steps of disassembly of VLP into pentamers and reassembly into VLP.

Abstract: A method of quantifying the amount of at least two analytes A1 and A2 involving (a) adding at least one salt (S) to at least a portion (P1) of the sample comprising the at least two analytes A1 and A2, (b) ionizing at least a portion of the sample according to (a) thereby forming an analyte flow comprising the analytes A1 and A2 in ionized form, (c) separating the ionized analytes A1 and A2 from each other by using at least one ion mobility separator (124), wherein the analyte flow according to (b) at least partially passes through the ion mobility separator (124), and (d) quantifying the amount of the separated ionized analytes obtained according to (c), wherein A1 is a pharmaceutically active compound C or derivative thereof and A2 is a metabolite or stereoisomer of C.

Abstract: A method of operating a chromatography column is described for use in methods of manufacture for producing anti-IL-12/IL-23p40 antibodies, e.g., the anti-IL-12/IL-23p40 antibody STELARA® (ustekinumab). This method involves collecting column outlet signal and accumulated flow parameters at two or more intervals of at least one mobile phase transition front during operation of the chromatography column comprising column packing. A model gamma cumulative distribution curve is calculated based on the collected column outlet signal and accumulated flow parameters for the at least one mobile phase transition front. A height equivalent theoretical plate (HETP) value is calculated for the at least one mobile phase transition front using parameters of the model gamma cumulative distribution curve and the quality of the chromatography column packing is assessed based on the calculated HETP value.

Abstract: A bispecific tetravalent antibody comprising an IgG having a pair of heavy chains and a pair of light chains, and two scFv components being connected to either C or N terminals of the heavy or light chains. The bispecific tetravalent antibody may have a binding specificity for two different epitopes on HER2 receptor.

Abstract: A wash buffer comprising greater than 0 mM and less than about 500 mM arginine, greater than 0 mM and less than about 250 mM guanidine, greater than 0 mM and less than about 250 mM sodium chloride, and greater than 0 mM and less than about 50 mM of an anionic surfactant, or greater than 0% and less than about 0.25% w/v of a non-ionic surfactant. When used during affinity chromatography purification of a protein of interest, such as an antibody, the wash buffer significantly reduces the level of host cell proteins from the preparation. Following affinity chromatography with the wash buffer, the protein of interest may be further purified using membrane chromatography.

Abstract: The present invention provides novel and improved protein purification processes which incorporate certain types of carbonaceous materials and result in effective and selective removal, of protein, fragments without adversely affecting the yield of the desired protein product.

Abstract: Purified recombinant polypeptides isolated from Chinese hamster ovary host cells, including antibodies, such as therapeutic antibodies, and methods of making and using such polypeptides are provided.

Abstract: The present invention discloses methods of neutralizing apatite surfaces, for example after a flow-through collection of a target and prior to cleaning the chromatography solid support.

Abstract: A method for producing a protein adsorbent comprising a substrate and a molecular chain fixed on the surface of the substrate is disclosed. The method comprises, in this order: a dry-heat treatment step of heating a pretreatment adsorbent comprising the substrate and the molecular chain fixed on the surface of the substrate, in which the molecular chain contains a weak electrolytic ion-exchange group; and a wet-heat treatment step of heating the pretreatment adsorbent in a moistened state with a liquid or steam to obtain the protein adsorbent.

Abstract: A process for obtaining human derived embryoid bodies (hEB). Human embryonic stem cells are incubated in vitro in a liquid growth medium under conditions in which the cells undergo differentiation, but do not adhere to the walls of the container. The invention also provides hEBs obtained by the process.

Abstract: A method is disclosed for purifying an antibody monomer, comprising providing a porous membrane comprising a hydrophobic porous substrate, a hydrophilic molecular chain of a different material from that of the porous substrate, immobilized on the surface of pores of the porous substrate, and a side chain of the molecular chain, containing a nitrogen atom to which one to three alkyl groups each having two or three carbon atoms are bonded; passing an antibody solution containing antibody aggregates of dimers or higher-order multimers through the porous membrane to adsorb the antibody aggregates to the porous membrane; and recovering the purified antibody monomer in the passed solution.

Abstract: The present invention pertains to improved methods of using dye-ligand affinity chromatography for the isolation of antibodies or proteins comprising an antibody fragment (such as Fc fusion proteins) from a mixture of undesirable contaminants. In particular, the use of an organic polymer such as polyethylene glycol (PEG) in the elution phase of an antibody/dye-ligand chromatography isolation procedure results in improved separation of target antibodies from undesirable contaminants. The methods described herein are particularly useful in separating or removing antibody aggregates, misfolded antibodies, and virus contaminants from target antibodies.

Abstract: The invention discloses a method of separating a biomolecule from at least one other component in a liquid, comprising a step of contacting said liquid with a separation matrix comprising a solid support and polymer chains bound to said solid support. The polymer chains comprise units derived from a first monomer of structure CH2?CH-L-X, where L is a covalent bond or an alkyl ether or hydroxysubstituted alkyl ether chain comprising 2-6 carbon atoms, and X is a sulfonate or phosphonate group.

Abstract: The present invention relates to a method to improve the sorbent efficiency of protein A chromatography using switching column with continuous feeding. In the chromatography method of the present invention, the increased usage efficiency of the absorbent (resin), the decreased processing time, the decreased operation cycle of column compared to that of single batch-type column, and the reduced amount of used resin are achieved and thus, the target protein can be purified at a high efficiency and a low cost.

Abstract: The invention relates to an immunoglobulin composition reduced in thrombogenic agents and to methods for its preparation. One method comprises subjecting an immunoglobulin containing solution to a negative cation exchanger chromatography at a pH in the range of higher than 3.8 to equal to or lower than 5.3. The solution can also be subjected to a negative anion exchanger chromatography at a pH in the range of 7 to 8.2.

Abstract: Disclosed herein are methods for the isolation and purification of antibodies wherein the use of an affinity chromatographic step results in an antibody composition sufficiently pure for pharmaceutical uses. The methods described herein comprise pH viral reduction/inactivation, ultrafiltration/diafiltration, affinity chromatography, preferably Protein A affinity, ion exchange chromatography, and hydrophobic chromatography. Further, the present invention is directed toward pharmaceutical compositions comprising one or more antibodies of the present invention.

Abstract: A method and system is provided for yielding biopharmaceutical products involving a chromatographic separation process. The method comprises: providing a plurality of membrane adsorber cartridges; providing a plurality of valves, communicatively coupled to said plurality of membrane adsorber cartridges; and switching the valves, so as to interconnect said membrane adsorber cartridges to operate in a countercurrent flow mode. The system comprises multiple membrane adsorber cartridges that are interconnected and configured to operate in a countercurrent flow mode. Furthermore, the configuration comprises a valve assembly that allows the cartridges to be subjected to different steps in the process by automatic switching of the valves. In this way, cartridges are recycled many times during the purification of a batch.

Abstract: The present invention provides methods for cleaning or regenerating a chromatography materiel for reuse. The methods of the invention can be used for cleaning or regenerating chromatography columns for reuse in the large-scale manufacture of multiple polypeptide products.

Abstract: Described herein are compositions and methods for treating, preventing and ameliorating diseases and conditions characterized by a lower than normal white blood cell count, such as leukopenia and neutropenia. The compositions and methods include recombinant human albumin-human granulocyte colony stimulating factor. Pharmaceutical formulations including the recombinant fusion protein, and methods of making such formulations are also described.

Abstract: Disclosed herein are methods and compositions for purifying proteins from crude solutions.

Abstract: The present invention provides a tag peptide comprising an amino acid sequence represented by the following formula (I): X1-Tyr-X2-Gly-Gln-X3??(I) (wherein X1, X2 and X3 are the same or different and each represent any amino acid residue) and an antibody against the tag peptide. By combined use of the tag peptide and antibody of the present invention, a system that enables proteins expressed from cloned genes to be highly purified in an inexpensive and easy manner can be established.

Abstract: The present invention relates to a chimeric inhibitor protein of a protease comprising an inhibiting polypeptidic sequence and at least one polypeptidic sequence of a substrate-enzyme interaction site specific for a protease. Other objects of the invention are to provide a purified and isolated DNA sequence encoding the chimeric inhibitor protein of a protease, an expression vector characterized in that it comprises said purified and isolated DNA sequence, a eukaryotic or prokaryotic host cell transformed with this expression vector and a method of producing a chimeric inhibitor protein.

Abstract: Purified genes encoding a T cell surface antigen from a mammal, reagents related thereto including purified proteins, specific antibodies, and nucleic acids encoding this antigen are provided. Methods of using said reagents and diagnostic kits are also provided.

Abstract: The invention is directed to an apparatus and method for purifying a protein. The apparatus involves the use of a capture chromatography resin, a depth filter arranged after the capture chromatography resin, and a mixed-mode chromatography resin arranged after the depth filter. The method involves providing a sample containing the protein, processing the sample through a capture chromatography resin, a depth filter, and a mixed-mode chromatography resin. A membrane adsorber or monolith may be substituted for the mixed-mode chromatography column.

Abstract: Fully human monoclonal Abs includes (i) an antigen-binding variable region that exhibits very high binding affinity for IL-1? and (ii) a constant region that is effective at both activating the complement system though C1q binding and binding to several different Fc receptors.

Abstract: A process for manufacturing of a composition containing a purified factor for supporting wound healing selected from the group consisting of Hepatocyte Growth Factor (HGF) platelet derived growth factor (PDGF), Epidermal growth factor (EGF), transforming growth factor alfa (TGF-?), Transforming growth factor beta (TGF-?), insulin like growth factor (IGF-I) and Fibroblast growth factor (FGF) from sources, such as blood, containing the factor for supporting wound healing, wherein the manufacturing process comprises purification steps which are performed in the presence of antithrombin III (AT-III).

Abstract: A method of refolding proteins expressed in non-mammalian cells present in concentrations of 2.0 g/L or higher is disclosed. The method comprises identifying the thiol pair ratio and the redox buffer strength to achieve conditions under which efficient folding at concentrations of 2.0 g/L or higher is achieved and can be employed over a range of volumes, including commercial scale.

Abstract: Expression vector systems are provided for increased production of a recombinant GDF-5 (rhGDF-5) protein. Also provided are transformed host cells that were engineered to produce and express high levels of rhGDF-5 protein. Methods for production and high expression of rhGDF-5 protein are disclosed herein. The methods of enhancing production and protein expression of rhGDF-5 protein as disclosed are cost-effective, time-saving and are of manufacturing quality.

Abstract: The invention provides, inter alia, multilayer films of alternating layers of a glycosylated polymer (e.g. a mucin) and a lectin, as well as methods of making and using these films. The films can be adapted for, inter alia, delivery of a biologically active agent providing a non-toxic substrate to support cell growth, replication, and/or maintenance as well as detecting a microorganism and/or reducing microorganism adherence to a surface.

Abstract: Methods of purifying proteins expressed in non-mammalian expression systems in a non-native soluble form directly from cell lysate are disclosed. Methods of purifying proteins expressed in non-mammalian expression systems in a non-native limited solubility form directly from a refold solution are also disclosed. Resin regeneration methods are also provided.

Abstract: The invention provides a process for preparing a cell-binding agent chemically coupled to a drug. The process comprises covalently attaching a linker to a cell-binding agent, a purification step, conjugating a drug to the cell-binding agent and a subsequent purification step.

Abstract: The present invention provides a new method for isolation and/or purification of immunoglobulins from a solution containing one or more immunoglobulins using a solid phase matrix represented by the formula: M-SP-L, wherein M is designates a matrix backbone, SP designates a spacer and L designates a substituted benzimidazole ligand.

Abstract: The present invention pertains to an affinity tag system for the immobilisation and/or purification of molecules such as biological or organic molecules. The invention provides EF-hand subdomains of calcium binding proteins, such as calbindin D9k, as affinity tags and affinity ligands for immobilising, detecting and/or for purifying molecules, particularly proteins. Also provided are methods utilising the affinity tag system of the invention, affinity matrices comprising EF-hand subdomain affinity ligands and fusion proteins comprising EF-hand subdomain affinity tags.

Abstract: Protein A crystals and Protein A cross-linked protein crystals (CLPCs) are described. Methods of preparing and using are also disclosed.

Abstract: Methods are provided for the prevention, treatment and diagnosis of Alzheimer's disease, based on the glycosylation pattern of amyloid-beta peptides in body fluids and tissues.

Abstract: Methods of expressing LIM mineralization protein in mammalian cells are described. Methods of expressing LIM mineralization protein and assessing glycosylation of the LIM mineralization protein in prokaryotic and non-mammalian eukaryotic cells are also described. The methods involve transfecting the cells with an isolated nucleic acid comprising a nucleotide sequence encoding a LIM mineralization protein. Transfection may be accomplished in vitro, ex vivo or in vivo by direct injection of virus or naked DNA, or by a nonviral vector such as a plasmid.

Abstract: Removal of genomic DNA from biological samples using cation exchange is described.

Abstract: The present invention provides a chromatography packing material having improved flow rate characteristics and adsorption characteristics. In particular, the present invention provides a chromatography packing material suitable for separation and purification of immunoglobulin in the manufacture of antibody preparations. A porous cellulose gel, which is made by adding polysaccharides having a limiting viscosity of 0.21 to 0.90 dL/g to porous cellulose particles, the dry weight per unit volume of the porous cellulose gel being 1.06 to 1.40 times the dry weight per unit volume of the porous cellulose particles, is used. By adding a predetermined amount of polysaccharides having a predetermined limiting viscosity to porous cellulose particles, flow rate characteristics and adsorption characteristics can be improved.

Abstract: Methods of enhancing efficiency of downstream chromatography steps for purification of proteins comprising: (a) passing a composition comprising a polypeptide of interest and various contaminants through an ion exchange membrane, wherein the polypeptide and the membrane have opposite charge, at operating conditions comprised of a buffer having a pH sufficiently distinct from the pi of the polypeptide to enhance the charge of the polypeptide and a low ionic strength effective to prevent the shielding of charges by buffer ions, which cause the membrane to bind the polypeptide and at least one contaminant, (b) overloading the ion exchange membrane such that at least one contaminant remains bound to the membrane while the polypeptide of interest is primarily in the effluent; (c) collecting the effluent from the ion exchange membrane comprising the polypeptide of interest; (d) subjecting the membrane effluent comprising the polypeptide of interest to a purification step of similar charge as the previous membrane,

Abstract: The present invention relates to a chromatography ligand defined by the following formula R1—R2—N(R3)—R4—R5 wherein R1 is a substituted or non-substituted phenyl group; R2 is a hydrocarbon chain comprising 0-4 carbon atoms; R3 is a hydrocarbon chain comprising 1-3 carbon atoms; R4 is a hydrocarbon chain comprising 1-5 carbon atoms; and R5 is OH or H. The invention also comprises a separation matrix, comprising the described ligands coupled to a porous support, such as particles or a membrane. The ligand and matrix according to the invention is useful for purification of biomolecules or organic compounds, such as proteins, polypeptides, DNA etc. An advantageous use according to the invention is the purification of antibodies.

Abstract: Disclosed herein are methods for the isolation and purification of antibodies wherein the use of an affinity chromatographic step results in an antibody composition sufficiently pure for pharmaceutical uses. The methods described herein comprise pH viral reduction/inactivation, ultrafiltration/diafiltration, affinity chromatography, preferably Protein A affinity, ion exchange chromatography, and hydrophobic chromatography. Further, the present invention is directed toward pharmaceutical compositions comprising one or more antibodies of the present invention.

Abstract: The invention is a method for the purification of mono-PEGylated erythropoietin using two cation exchange chromatography steps wherein the same type of cation exchange material is used in both cation exchange chromatography steps and a method for producing a mono-PEGylated erythropoietin in substantially homogeneous form.