The present invention provides methods for producing antibodies against peptides, proteins, or such to which immune tolerance is easily established, by using antigen-binding molecules comprising a domain that binds to a molecule expressed on the surface of a cell having an immune response-suppressing function and a T cell receptor (TCR) complex-binding domain. The present invention also provides pharmaceutical compositions for use in combination with therapeutic vaccines and agents for enhancing a humoral immune response, each comprising the antigen-binding molecules as active ingredients.

It was discovered that, by preparing an Fc region of an Fc region-containing polypeptide in which the first polypeptide chain of the Fc region binds to a Protein A resin, but the second polypeptide chain of the Fc region does not bind to the resin or shows weak binding to it, the amount of the Fc region-containing polypeptide bound per volume of the resin is increased, and more efficient purification of the above-mentioned Fc region-containing polypeptide is possible.

The invention described herein relates to an improved method for analytical capillary gel electrophoresis (CGE) for complex biologic molecules. The methods for the improved CGE include steps for the partial reduction of the biologic analyte molecule for use as calibration standard and use such partially reduced calibration sample to obtain an improved calibration curve for CGE to be used with biologic analyte molecules.

Provided herein are, inter alia, biological manufacturing and downstream purification processes.

Herein is reported the use of an immobilized non-covalent complex of a neonatal Fc receptor (FcRn) and beta-2-microglobulin (b2m) as affinity chromatography ligand in general and, for example, for the determination of the in vivo half-live of an antibody by determining the ratio of the retention times of the antibody and a reference antibody.

The invention provides human plasma-derived immunoglobulin compositions comprising low levels of thrombogenic agents and of IgG aggregates. The invention further provides methods for removing the active coagulation factors and IgG aggregates content of a plasma-derived immunoglobulin composition.

The present invention discloses a method for the purification of Fc-fusion proteins from the contaminants. In particular, the disclosed method describes a process for the purification of Fc-fusion proteins using a specific order of chromatographic steps. The specific order of chromatography steps as disclosed results in reducing contaminants such as high-molecular weight aggregates and sialylated isoforms and obtaining a purified Fc-fusion protein composition.

Antibodies that specifically bind PD-1 or antigen binding fragments thereof, polynucleotides encoding the antibodies or fragments, and methods of making and using the foregoing are useful in the treatment of an inflammatory or immune disorder.

The present invention relates to an improved method of quantification and/or estimation of purity of antibody or fusion protein from a protein mixture containing impurity by providing long term sample stability. The invention provides a stable protein solution comprising antibody having reduce formation of Fab and Fc related impurities.

Provided herein are, inter alia, biological manufacturing and downstream purification processes.