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Roche Launches First Sugar-Transferase for New Glyco-Engineering Portfolio

Published: Monday, July 01, 2013
Last Updated: Monday, July 01, 2013
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Enzyme supports applications from research to Biopharmaceutical Manufacturing.

Roche announced the launch of its new alpha-2,6-Sialyltransferase for in vitro sialylation of glycoproteins and complex molecules as human monoclonal antibodies (mAbs). The enzyme, which is offered for research and pilot scale applications, is produced under animal-origin free conditions and offers a very high lot-to-lot consistency.

“This launch is the first in a series to offer a complete glyco-engineering portfolio of key enzymes and activated sugars covering a broad spectrum of applications,” said Ruedi Stoffel, Head of Biochemical Reagents & Custom Biotech. “The initial feedback from bio-manufacturing customers showed that our continuous scientific and technical support throughout the up-scaling and development process differentiates Roche as a strong partner.”

The alpha-2,6-Sialyltransferase delivers up to 95% bi-antennary sialylation of N-Glycan chains within 6 – 8 hours, a performance which is currently not offered by competitor products. It is based on a human genome sequence and expressed in mammalian expression systems. Over the coming months, Roche plans to complete the portfolio through launches of additional Sialyl-and Galactosyltransferases.

Glycosylation is considered to be one of the main sources of biologics’ heterogeneity and is seen as a critical quality attribute by regulatory bodies. The implementation of Quality by Design Standards in the manufacturing of Active Pharmaceutical Ingredients such as mAbs with specific glycosylation patterns is expected to play a central role in future bio-manufacturing processes.


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