Background

Control over glycosylation is a critical factor during recombinant therapeutic production because of its profound effect on protein function, allergenic and immunogenic properties, plasma clearance rates and efficacy. It is now accepted that specific glycan structures adversely affect the safety of these recombinant products. Currently analytical methods for detection and quantification of glycans are based on complex and expensive high-performance liquid chromatography (HPLC) and mass spectrometry (MS).

Technology Overview

Assays, utilizing single chain variable fragment (scFv) and aptamers for the detection of non-human Gal-a-(l→3)-Gal and both sialic acid common forms (N-glycolylneuraminic (Neu5Gc) acid and N-acetylneuraminic acid (Neu5Ac)) have been developed as both direct and composite ELISA formats, permitting detection and quantification of the target glycan epitope.

The present technologies consist of highly-specific antibody fragments with unmatched specificity and high affinity (>108) for a) non-human Gal-a-(l→3)-Gal epitope and b) sialic acids - Neu5Gc acid Neu5Ac, which have been developed into a rapid and convenient assay formats

Benefits

Convenient assay system
Rapid, robust molecules
Patent pending

Applications

Biopharmaceuticals
Glycobiology
Analytics
Food industry
Biologics
Pharmaceuticals

Opportunity

Available for licensing
Product development

Sugar Recognition Molecules

Patents

IP Status

Seeking