An object of the present invention is to provide, as a method for producing an antibody at a lower cost than the prior art, a method for purifying an antibody in a non-adsorption mode using an inorganic compound containing silicon dioxide and aluminum oxide, a method for producing an antibody comprising the purification method, and an antibody produced by the production method, and the like. The present invention relates to a method for purifying an antibody in a non-adsorption mode using an inorganic compound containing silicon dioxide and aluminum oxide, a method for producing an antibody comprising the purification method, and an antibody produced by the production method.

The present disclosure relates to methods of re-oxidizing an antigen-binding protein.

Disclosed herein are anti-Galectin-9 antibodies and methods of using such for inhibiting a signaling pathway mediated by Galectin-9 or eliminating pathologic cells expressing Galectin-9. Such anti-Galectin-9 antibodies may also be used to diagnose and/or to treat diseases associated with Galectin-9, such as autoimmune diseases and solid tumors.

Systems and methods to characterize dimerization interfaces at the subdomain level of a protein are provided. An exemplary method includes digesting a protein dimer sample into subdomains, labeling the digested protein sample, isolating labeled dimeric and monomeric subdomain fragments, and peptide mapping the labeled sample to determine where the dimer fragments are labeled and where the dimer fragments are not labeled. Regions that show decreased labeling extents in the dimer fraction than that in the monomer fraction are likely involved or in close proximity to the dimerization interface.

Provided in the present invention are a type of anti-human PD-L1 specific nanobodies and VHH chains thereof, coding sequences of the foregoing nanobodies or VHH chains thereof, corresponding expression vectors and host cells, and a method for producing antibodies.

Provided herein are formulations of PCSK9-binding polypeptides, such as those comprising evolocumab, that comprise N-acetyl arginine and have reduced viscosities when compared to formulations lacking N-acetyl arginine. Provided herein are also methods of formulating such compositions that are advantageous in that they conserve certain components. Such formulations comprising PCSK9-binding polypeptides can be administered to patients to treat and/or prevent PCSK9-related diseases, conditions, and disorders.

A process for synthesizing and separating secretory IgA from a mixture of IgA monmer and IgA dimer is provided. The process includes covalently binding affinity tagged or epitope tagged recombinant secretory component to the IgA dimer in the mixture and binding the affinity tagged or an epitope tagged secretory IgA to immobilized moieties on the solid phase support resin to which the affinity tag or epitope tag binds and then eluting the affinity tagged or an epitope tagged secretory IgA with release buffer. A process for synthesizing and separating secretory IgM from a mixture of IgM and other plasma proteins is also provided. The process includes covalently binding affinity tagged or an epitope tagged recombinant secretory component to the IgM in the mixture and binding the affinity tagged or an epitope tagged secretory IgM to immobilized moieties on the solid phase support resin and then eluting the peptide tagged secretory IgM with a release buffer.

The invention relates to a method of isolating an immunoglobulin, comprising the steps of: a) providing a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains covalently coupled to a porous support, b) contacting a liquid sample comprising an immunoglobulin with the separation matrix, c) washing said separation matrix with a washing liquid, d) eluting the immunoglobulin from the separation matrix with an elution liquid, and e) cleaning the separation matrix with a cleaning liquid,
wherein 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.

This present disclosure provides a process for concentrating proteins including an ultrafiltering, a diafiltering, and a second ultrafiltering sequence, at elevated temperatures, such as above about 30° C. The disclosure also includes a process of preparing highly concentrated antibody compositions. and highly concentrated antibody products.

Provided herein are methods of separating host cell lipases from an anti-LAG3 antibody or antigen binding fragment in chromatographic processes and methods of improving polysorbate-80 stability in an anti-LAG3 antibody formulation by separating host cell lipases from the anti-LAG3 antibody or antigen binding fragment using chromatographic processes. Also provided are pharmaceutical compositions comprising an anti-LAG3 antibody or antigen binding fragment and less than 2 ppm of a host cell lipase.