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Acetyl esterase for the characterisation of glycosylation in EPO

Ludger Ltd

Acetyl esterase (sialate-O-acetylesterase) is a useful tool to remove 9-, 8- and 7-O-acetyl groups from EPO biopharmaceutical glycans

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
phone +44 (0) 1865 408 554
email info@ludger.com
web www.ludger.com
email Ludger Ltd, Culham Science Centre, Abingdon, Oxfordshire, OX14 3EB
 
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