Acetyl esterase for the characterisation of glycosylation in EPO

Acetyl esterase (sialate-O-acetylesterase) is a useful tool to remove 9-, 8- and 7-O-acetyl groups from EPO biopharmaceutical glycans because these sugars and their acetylation are believed to be essential factors for the function, efficacy and half-life of the drug in patients.

This enzyme can also be used for the characterisation of other highly sialylated biotherapeutics such as FSH and blood clotting factors. Reference: Biochem J. 2015 Dec 1;472(2):157-67. doi: 10.1042/BJ20150388. Epub 2015 Sep 16.

A paper entitled Analysis of three epoetin alpha products by LC and LC-MS indicates differences in glycosylation critical quality attributes, including sialic acid content has been accepted for publication by Analytical Chemistry.

This work was the result of a collaboration between the University of Reading, University of Sheffield and Ludger and acetyl esterase was used for this study. Reference: Anal Chem. 2017 Jun 9. doi: 10.1021/acs.analchem.7b00353. [Epub ahead of print] PMID: 28509534

Acetyl esterase (sialate-O-acetylesterase) is available to order from Ludger. Kit containing enzyme and buffer sufficient for 50 samples (Cat No LZ-ACASE-KIT).

Recent Issues