MedImmune, LLC

Disclosed are methods for testing the presence and/or activity of glutathione system components and thioredoxin system components during the manufacturing process of disulfide bond-containing proteins. Also disclosed are methods for mitigating reduction of disulfide bonds during the manufacturing process, and for lowering the reduction potential of disulfide bond-containing proteins. Provided are compositions, kits, and methods for mitigating reduction and diminishing reduction potential of disulfide bond-containing proteins during protein manufacturing processes.

Provided herein are clonal Chinese Hamster Ovary (CHO) cells and their use in increasing cellular productivity in biomanufacturing processes. Specifically, the disclosure provides a method of improving specific cellular productivity of a polypeptide of interest in a recombinant cell comprising expressing a nucleic acid encoding the polypeptide of interest in a recombinant cell having a high mitochondrial membrane potential (MMP).

Provided herein is an environmentally compatible detergent for use in purification of a recombinantly produced bio-therapeutic. The environmentally compatible detergent includes Laureth-9 and can be used for viral clearance, cell lysis, and removal of impurities such as host cell proteins an endotoxins. Advantageously, Laureth-9 does not adversely impact product quality.

The present invention relates to improved pharmaceutical compositions that contain high concentrations of one or more protein biomolecule(s). In particular, the invention relates to pharmaceutical compositions that include an optimized ratio of protein biomolecule to an amorphous stabilizing compound or compounds, especially a sugar, such as sucrose, trehalose, glucose, lactose or sorbitol, or mixtures thereof, or one or more amino acid molecules such as arginine, alanine, glycine, lysine or proline, or derivatives and salts thereof, or mixtures thereof. The inclusion of such amorphous stabilizing compound(s), at such optimized ratio, provides acceptable long-term stability of the protein biomolecule, and facilitates shorter lyophilization time, more specifically shorter drying time, even more specifically shorter primary drying time.

The present invention relates to a method of purifying albumin-fusion proteins to reduce the level of oxidation of susceptible amino acid residues. The method comprises an affinity matrix chromatography step and an anion exchange chromatography step. The purified albumin-fusion proteins have low levels of oxidation and retain their enhanced half-life in vivo and its bioactivity. In some embodiments, the albumin-fusion protein comprises a scaffold, such as human Tenascin C scaffold. Compositions comprising the albumin-fusion protein are further disclosed.

This application provides improved cell culture media and cell culture methods comprising N-acetylcysteine. These improved cell culture media and cell culture methods increase cell viability, cellular growth rate and/or reduce cell doubling time of cholesterol auxotrophic cells, myeloma cells, and hybridoma cells.

This application provides improved cell culture media and cell culture methods comprising N-acetylcysteine. These improved cell culture media and cell culture methods increase cell viability, cellular growth rate and/or reduce cell doubling time of cholesterol auxotrophic cells, myeloma cells, and hybridoma cells.

The present disclosure relates to a process for preparing antibodies with a defined glycosylation pattern, in particular antibodies with a glycan terminating in an N-acetylglucosamine. The antibodies of the disclosure are suitable for use in a process to conjugate a payload thereto. The disclosure also extends to molecules obtained and obtainable from the process disclosed herein, novel molecules and intermediates, compositions comprising said molecules and uses of the molecules and compositions, particularly in treatment, for example in the treatment of cancer.

Disclosed are methods for testing the presence and/or activity of glutathione system components and thioredoxin system components during the manufacturing process of disulfide bond-containing proteins. Also disclosed are methods for mitigating reduction of disulfide bonds during the manufacturing process, and for lowering the reduction potential of disulfide bond-containing proteins. Provided are compositions, kits, and methods for mitigating reduction and diminishing reduction potential of disulfide bond-containing proteins during protein manufacturing processes.

The present invention is directed to methods of screening populations of transgenic cells for cells that produce a protein of interest. The methods comprise culturing transgenic cells in culture conditions that include at least one non-natural amino acid (nnAA) in the cell culture medium. The transgenic cells comprise at least one polynucleotide that codes for a fusion protein with a first domain coding for a protein of interest and a second domain coding for a domain that facilitates detection of the transgenic cells that express the protein of interest when the transgenic cell expresses the second domain.