Abstract: 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.

Abstract: A method that uses Protein A chromatography to separate antigen-binding polypeptide monomers comprising one or more immunoglobulin single variable domains (ISVDs) from aggregates of said monomers is disclosed.

Abstract: The present invention provides Herpes Simplex Virus (HSV) gD, gC, gB and/or gE recombinant glycoproteins having a particular pre-selected N-linked glycosylation pattern as the predominant N-glycoform. The present invention also provides methods of producing these recombinant glycoproteins in yeast, preferably Pichia pastoris, which may be glycoengineered to provide particular glycosylation patterns. The present invention further provides vaccines comprising gD and gC, and optionally gB and/or gE, at least one of which has a particular pre-selected N-linked glycosylation pattern as the predominant N-glycoform. The recombinant glycoproteins are produced by a method which, in one embodiment, comprises transforming a yeast of the genus Pichia with an expression vector containing a DNA encoding an HSV glycoprotein, which is under regulation of a promoter functional in a yeast of the genus Pichia, culturing the yeast in a medium, and recovering the recombinant glycoprotein from the obtained culture.