Amgen Inc.

Arizona State University

Douglas Rehder

Pavel V Bondarenko

Chad Borges

Arnold McAuley

Margaret Ricci

Thomas M Dillon

Dirk Chelius

Matthew Schaab

Masazumi Matsumura

Arnold Mcauley

Yuefeng Lu

Joe Zhou

Yuling Zhang

Himanshu S Gadgil

Douglas D Banks

Andrew Goetze

Gary Pipes

Gerd Kleemann

Douglas Banks

Thomas Dillon

Pavel Bondarenko

The present disclosure provides a method for analyzing glyeart-derived monosaccharides in a sample. The present disclosure also provides a method for detecting or monitoring a disease or disorder in a patient. In addition, the present disclosure provides a method of determining aberrant glycotransferase activity. The present disclosure further provides a system for analyzing or comparing glycates in a sample.

Methods for analyzing glycan-derived monosaccharides

Methods for quantifying biospecimen sample integrity using markers of oxidation (FIG.). Under conditions of incomplete blood plasma/serum (P IS) sample freezing (including storage at &#x2212;20 ?C), two different forms of oxidation occur spontaneously at protein sulfur atoms&#x2014;namely S-cysteinylation of free cysteine residues (in which the oxidative event is disulfide bond formation) and sulfoxidation of methionine. Oxidized forms of albumin and apoA-1, SCA and MOA1 are useful markers of biospecimen integrity. The oxidative chemistries of SCA and MOAI are operational in other proteins and polypeptides. Thus, for rare cases in which the use of SCA or MOA1 may be contraindicated, custom designed surrogate peptide probes based on SCA and MOA1 oxidation chemistry may be fortified into samples at collection to serve as exogenous markers of P/S sample integrity.

Methods for assessing biospecimen integrity

The present invention provides reagents and methods for limiting adsorptive and/or oxidative protein losses in a sample.

Buffers for stabilizing biological specimens and their use

The invention provides a formulation including a buffer having a pH less than 6.0, a divalent cation between about 5-200 mM, an excipient comprising a sugar or polyol and an effective amount of a therapeutic polypeptide. Also provided is a method of stabilizing a polypeptide. The method includes contacting a therapeutic polypeptide with a concentration of divalent cation between about 5-150 150 mM in a buffer having a pH less than 6.0 and an excipient comprising a sugar or polyol.

Stable polypeptide formulations

The present invention is generally directed to methods of producing an increase in the enrichment or recovery of preferred forms of IgG proteins. More particularly, the invention relates to subjecting preparations of such recombinant IgG proteins with a reduction/oxidation coupling reagent and optionally a chaotropic agent.

Methods for refolding of recombinant antibodies

The present invention is directed to a novel method of analysis of high molecular weight proteins. More specifically, it is directed to a novel reversed-phase LC/MS method of analysis of high molecular weight proteins including antibodies.

LC/MS method of analyzing high molecular weight proteins

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Phoenix, AZ, United States of America

Douglas Rehder