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Displaying 26 - 50 of 66

NIST Spectroscopic Measurement Standards

May 1, 2018
Author(s)
Paul C. DeRose, Kenneth D. Cole, Aaron Urbas, Steven J. Choquette, Evelyn Solis, Erica V. Stein, John E. Schiel, Brian Lang, Hua-Jun He
Ultraviolet (UV) absorbance measurements provide a rapid and reliable method to determine protein concentrations. The National Institute of Standards and Technology (NIST) has developed Standard Reference Material (SRM) 2082as a pathlength standard for UV

The role of mass spectrometry in the characterization of biologic protein products

April 25, 2018
Author(s)
Deepali Rathore, John E. Schiel, Anneliese Faustino, Eric Pang, Michael Boyne, Sarah M. Rogstad
Introduction: Mass spectrometry (MS) is widely used in the characterization of biomolecules including peptide and protein therapeutics. These biotechnology products have seen rapid growth over the past few decades and continue to dominate the global

Qualification of NISTmAb charge heterogeneity control assays

March 18, 2018
Author(s)
Abigail Turner, John E. Schiel
The NISTmAb is a monoclonal antibody Reference Material from the National Institute of Standards and Technology; it is a class-representative IgG1κ intended serve as a pre-competitive platform for harmonization and technology development in the

Development of an LC-MS/MS peptide mapping protocol for the NISTmAb

March 1, 2018
Author(s)
Catherine A. Mouchahoir, John E. Schiel
Peptide mapping is a component of the analytical toolbox used within the biopharmaceutical industry to aid in the identity confirmation of a protein therapeutic and to monitor degradative events such as oxidation or deamidation. These methods offer the

The NISTmAb Reference Material 8671 Value Assignment, Homogeneity, and Stability

March 1, 2018
Author(s)
John E. Schiel, Abigail Turner, Catherine A. Mouchahoir, Katharina S. Yandrofski, Srivalli Telikepalli, Jason King, Paul C. DeRose, Dean C. Ripple, Karen W. Phinney
The NISTmAb Reference Material (RM) 8671 is intended to be the common industry standard monoclonal antibody for pre-competitive research in harmonizing current state-of-the-art technology and designing next generation characterization technologies for

Development of Orthogonal NISTmAb Size Heterogeneity Control Methods

February 10, 2018
Author(s)
Abigail Turner, Katharina S. Yandrofski, Srivalli Telikepalli, N. Alan Heckert, James J. Filliben, Dean C. Ripple, John E. Schiel
The NISTmAb is an innovative monoclonal antibody reference material from the National Institute of Standards and Technology; it is a class-representative IgG1κ intended to serve as a pre-competitive platform for harmonization and technology development in

Determination of the Primary Sequence/ Structure

October 15, 2015
Author(s)
Catherine A. Mouchahoir, Mellisa Ly, Michaella Levy, Lisa E. Kilpatrick, Scott C. Lute, Karen W. Phinney, Lisa Marzilli, Kurt A. Brorson, Michael T. Boyne, Darryl Davis, John E. Schiel
The primary sequence of a protein, including therapeutic monoclonal antibodies (mAbs), is a critical quality attribute that determines a great deal of its functionality and stability. Significant effort is devoted to determining the complete amino acid

Glycan Analysis of NIST mAb Reference Material

October 15, 2015
Author(s)
John E. Schiel, Catherine A. Mouchahoir
N-linked glycosylation is a common post-translational modification that imparts structural heterogeneity to recombinant monoclonal antibody therapeutics. The various oligosaccharides attached to the CH2 domains of IgG can impact the efficacy, safety and

Structural Elucidation of Chemical and Post-translational Modifications of Monoclonal Antibodies

October 15, 2015
Author(s)
Wenzhou Li, James L. Kerwin, John E. Schiel, Catherine A. Mouchahoir, Darryl Davis, Andrew Mahan, Sabrina A. Benchaar
Therapeutic monoclonal antibodies (mAbs), a rapidly growing class of therapeutic drugs, present a daunting challenge for structural characterization. They are heterodimers of separate light and heavy chains comprising over 1200 amino acid residues. During