A method for manufacturing a mixed-mode chromatography medium is provided. The method can include, for example, oxidizing diol groups on diol-functionalized solid particles having pores of a median diameter of 0.5 micron or greater with substantially no pores of 0.1 micron or less in diameter and having a diol density of from about 200 to about 300 μmol/mL to aldehyde groups, thereby converting said diol-functionalized solid particles to aldehyde-functionalized solid particles; and coupling amine-functionalized ligands to said aldehyde-functionalized solid particles, said amine-functionalized ligands comprising an amine-substituted hydrophobic group joined to an acid moiety selected from the group consisting of a carboxyl group and a sulfo group.

The present invention relates to a method and a system of extracting a protein with high yield from a protein-comprising precipitate, in particular immunoglobulin, from human or non-human origins, such as blood plasma.

The present invention relates to a method and a system of extracting a protein with high yield from a protein-comprising precipitate, in particular immunoglobulin, from human or non-human origins, such as blood plasma.

The present invention is in the field of purification and protein purification in particular. The invention provides improved techniques for the industrial-scale purification of proteins and other biomolecules. More specifically, it relates to a process for the purification of a compound of interest, such as a protein, preferably an antibody or an antibody fragment using a chromatography step, preferably a semi-continuous chromatography step.

The disclosure provides systems and methods useful for predicting or detecting a malfunction in a chromatography process in real-time. In some embodiments, the disclosure provides systems and methods for detecting an atypical profile in a process chromatogram in ion-exchange chromatography of a biologic product.

The disclosure provides systems and methods useful for predicting or detecting a malfunction in a chromatography process in real-time. In some embodiments, the disclosure provides systems and methods for detecting an atypical profile in a process chromatogram in ion-exchange chromatography of a biologic product.

The current invention is based, at least in part, on the finding that the transverse nuclear magnetic spin relaxation time T2 and the transverse nuclear magnetic spin relaxation rate R2, respectively, of protons of water molecules in an aqueous solution comprising viral particles depends on the loading status (full vs. empty) of the viral particle. Thus, one aspect of the current invention is a method for determining the ratio of loaded viral particles to empty viral particles in a sample, comprising the steps of determining a nuclear magnetic resonance (NMR) parameter related to the protons of the water molecules present in an aqueous solution comprising a mixture of loaded and empty viral particles by applying an NMR measurement to the solution, and determining the ratio of loaded viral particles to empty viral particles with the NMR parameter determined in the previous step based on a calibration function.

The present disclosure pertains to compositions comprising anti-VEGF and methods for producing such compositions in chemically defined media and controlling amounts of certain oxidized aflibercept variants.

The present disclosure pertains to compositions comprising anti-VEGF and methods for producing such compositions in chemically defined media and controlling amounts of certain oxidized aflibercept variants.

Disclosed herein are methods and exemplary compositions associated with virus purification, antigen purification, and conjugation of virus and proteins (e.g., antigen) to form vaccines for delivery of immunological and other therapeutic agents, exemplary aspects of which may include harvesting viral and antigenic substances from source organisms; a purification platform comprising chemical separation and size-difference separation for the removal of contaminants, debris and impurities from the viral and protein (e.g. antigenic, including influenza hemagglutinin antigens) substances, as well as their concentration and collection; and a conjugation platform providing activation of the virus at a pH that increases binding rate and binding propensity between the virus and the protein, wherein embodiments related to the conjugation platform include controlling the ratio of virus to protein.