Abstract: Eculizumab, a humanized monoclonal antibody against C5 that inhibits terminal complement activation, showed activity in a preliminary 12-week open-label trial in a small cohort of patients with paroxysmal nocturnal hemoglobinuria (PNH). The present study examined whether chronic eculizumab therapy could reduce intravascular hemolysis, stabilize hemoglobin levels, reduce transfusion requirements, and improve quality of life in a double-blind, randomized, placebo-controlled, multi-center global Phase III trial. It has been found that eculizumab stabilized hemoglobin levels, decreased the need for transfusions, and improved quality of life in PNH patients via reduced intravascular hemolysis. Chronic eculizumab treatment appears to be a safe and effective therapy for PNH.

Abstract: Described herein is secretory IgA isolated from the intestinal luminal fluid and intestinal mucosal of animals such as pigs and cows. Also included are methods of isolating secretory IgA. The secretory IgA is useful in food compositions such as animal and human food compositions as well as pharmaceutical compositions to increase growth rate, improve feed efficiency, reduce gastrointestinal inflammation, reduce a risk of gastrointestinal infection in the animal, or a combination thereof.

Abstract: Combinations of different chromatography modalities with particularly refined conditions significantly reduce acid charge variants in a preparation of monoclonal antibodies. The process for reducing acid charge variants utilizes a combination of anion exchange and hydrophobic interaction chromatography, followed by cation exchange chromatography polishing, whereby the levels of acidic or basic charge species of the monoclonal antibodies may be modulated to a desired level.

Abstract: In certain embodiments, the invention provides a method of purifying a protein of interest from a mixture which comprises the protein of interest and one or more contaminants, said method comprising: a) subjecting the mixture to a first chromatography matrix, wherein the protein of interest binds to the first chromatography matrix; b) contacting the first chromatography matrix with a first wash solution which has a pH of at least 9.0, and does not comprise arginine or an arginine derivative; and c) eluting the protein of interest from the first chromatography matrix into an elution solution.

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: A method for purifying a protein comprising an antibody, antibody fragment, or immunoglobulin single variable domain, from a solution containing at least one contaminant by superantigen chromatography comprising: a) adsorbing the protein to the superantigen immobilized on a solid support; b) removing the at least one contaminant by contacting the immobilized superantigen containing the adsorbed protein with a first wash buffer comprising an aliphatic carboxylate; and c) eluting the protein from the superantigen immobilized on the solid support.

Abstract: Provided herein are de novo binding domain containing polypeptides (DBDpp) that specifically bind a target of interest. Nucleic acids encoding the DBDpp, and vectors and host cells containing the nucleic acids are also provided. Libraries of DBDpp, methods of producing and screening such libraries and the DBDpp identified from such libraries and screens are also encompassed. Methods of making and using the DBDpp are additionally provided. Such uses include, without limitation, affinity purification, and diagnostic and therapeutic applications.

Abstract: The present inventors discovered that additional aggregation of low-pI antibody can be suppressed by removing formed antibody aggregates after a certain period of time following Protein A column purification, acidic treatment, and neutralization. Furthermore, the present inventors found that efficient impurities removal for a low-pI antibody can be accomplished by using an anion exchange resin in the Bind/Elute mode and then a hydrophobic interaction chromatography or multimodal chromatography resin, compared with conventional methods.

Abstract: Disclosed herein are methods that have been developed to control the formation of disulfide bonds between polypeptides of a multimeric protein produced by a bioprocess. Also disclosed are protein solution parameters that allow for controlling the formation of disulfide bonds. In one example, the methods disclosed herein can be used to control the proportion of half antibody molecules in an antibody solution.

Abstract: Provided herein are de novo binding domain containing polypeptides (DBDpp) that specifically bind a target of interest. Nucleic acids encoding the DBDpp, and vectors and host cells containing the nucleic acids are also provided. Libraries of DBDpp, methods of producing and screening such libraries and the DBDpp identified from such libraries and screens are also encompassed. Methods of making and using the DBDpp are additionally provided. Such uses include, without limitation, affinity purification, and diagnostic and therapeutic applications.

Abstract: A human antibody ? type light chain complex-containing composition includes a complex in which a human antibody ? type light chain is bound to one or more kinds of metal ions selected from the group consisting of Group 10 elements, Group 11 elements, and Group 12 elements. The human antibody ? type light chain is a dimer, cysteines at C terminals of two human antibody ? type light chains are bound to each other via the metal ion, and 0.1 mol or more of the metal ion is bound per 1 mol of the human antibody ? type light chain.

Abstract: The present invention provides a novel method for manufacturing a protein, particularly where said protein is to be coupled with another molecule. The invention further provides a method for industrial scale protein manufacturing to obtain proteins, e.g., for therapeutic purposes.

Abstract: High resolution protein A chromatography employing a chaotropic agent and pH gradient or pH step elution buffer results in improved peak resolution between closely related molecular species. Bispecific antibodies containing a protein A-binding-ablating substitution CH3 domain paired with a protein A-binding CH3 domain are separated with high peak resolution from monospecific antibodies containing a protein A-binding-ablating substituted CH3 domain paired with the protein A-binding-ablating substituted CH3 domain and monospecific antibodies containing a protein A-binding CH3 domain paired with the protein A-binding CH3 domain. Useful chaotropic agents include magnesium chloride and calcium chloride.

Abstract: Eculizumab, a humanized monoclonal antibody against C5 that inhibits terminal complement activation, showed activity in a preliminary 12-week open-label trial in a small cohort of patients with paroxysmal nocturnal hemoglobinuria (PNH). The present study examined whether chronic eculizumab therapy could reduce intravascular hemolysis, stabilize hemoglobin levels, reduce transfusion requirements, and improve quality of life in a double-blind, randomized, placebo-controlled, multi-center global Phase III trial. It has been found that eculizumab stabilized hemoglobin levels, decreased the need for transfusions, and improved quality of life in PNH patients via reduced intravascular hemolysis. Chronic eculizumab treatment appears to be a safe and effective therapy for PNH.

Abstract: The present invention provides a method for preparing a composition comprising highly concentrated antibodies by ultrafiltration in batch concentration mode having a first constant feed rate step and a second controlled feed rate step.

Abstract: An object of the present invention is to provide a Fab region-binding peptide having an excellent ability for binding to a Fab region of IgG, an affinity separation matrix having the peptide as a ligand, and a method for producing a Fab region-containing protein, the method using the affinity separation matrix. Further, another object of the present invention is to provide a DNA encoding for the peptide, a vector containing the DNA, and a transformant which has been transformed by the vector. The Fab region-binding peptide according to the present invention is characterized in having a mutation at a specific site in comparison with wild-type SpG-?1.

Abstract: The first embodiment of the present invention is a method for purifying an antibody or a substance derive from an antibody, wherein a carrier 1 having an affinity ligand with affinity for the antibody or the substance derived from the antibody and a carrier 2 having a cation exchange group are used to prepare an integrated column 1 connecting a column containing the carrier 1 and a column containing the carrier 2 or a column 2 having the mixture of the carrier 1 and carrier 2, the antibody or the substance derived from the antibody is applied to the column 1 or the column 2, and then the adsorbed antibody or substance derived from the antibody is eluted from the column 1 or the column 2. The second embodiment of the present invention is a method for using a carrier having a cation exchange group, wherein a solution containing an antibody or a substance derived from an antibody is applied to a carrier having a cation exchange group having a carboxyl group-containing ligand and pKa of 4.

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: This application relates to methods for purification of proteins such as antibodies using a hydrophilic polymer (e.g., PEG), a fatty acid (e.g., caprylic acid), and/or another agent (e.g., calcium chloride).

Abstract: This disclosure relates to methods for isolating antibodies from cell-free culture supernatant.