Well-characterized reference materials enable successful collaborations within the scientific community by establishing common reagents for benchmarking studies and reducing the barriers to sharing materials and information. Here, we report the development of NISTCHO, a recombinant Chinese hamster ovary cell line expressing a nonoriginator version of the NISTmAb IgG1. We evaluated candidate clonal cell lines in a fed-batch cell culture model to assess growth and productivity of the cell lines...

Photo-stability represents a critical quality attribute for the development of therapeutic proteins where the exposure to near UV or visible light can lead to protein fragmentation. Here, we compare the photo-stability of three IgG1 based modalities, formulated in histidine (His) buffer containing various levels of Fe(III). We report a significant difference in the extent of photo-degradation between a high mannose Fc fragment (HM-Fc), NISTmAb and a fusion protein, Flt-3L-Ig. Our results...

NISTCHO is a Chinese hamster ovary (CHO) cell line expressing the same amino acid sequences as the heavy and light chains of the National Institute of Standards and Technology (NIST) monoclonal antibody [Reference Material (RM) 8671 NISTmAb]. NISTCHO was generated by MilliporeSigma to be developed by NIST as a RM to support biomanufacturing research and innovation, method development and qualification, and pre-competitive research collaboration. The RM cell line, denoted as RM 8675 NISTCHO,...

Antibody-based therapeutics have demonstrated remarkable therapeutic benefit, but their susceptibility to biotransformation and degradation in the body can affect their safety, efficacy, and pharmacokinetic/pharmacodynamic (PK/PD) profiles. In vitro stability assessments play a pivotal role in proactively identifying potential liabilities of antibody therapeutics prior to animal studies. Liquid chromatography-mass spectrometry (LC-MS)-based in vitro stability assays has been developed and...

A comprehensive characterization of biotherapeutics, mandated by regulatory authorities, requires analyses of a protein drug at multiple structure levels. Such multilevel characterization can be performed by mass spectrometry (MS), with established conventional MS-based assays of product quality attributes (PQAs) comprising intact protein and subunit middle-up MS with analytes resolved on a C4 column, and bottom-up peptide mapping with analytes resolved on a C18 column. Recent advances in MS...