Targeting allosteric disulphide bonds in cancer.

Nature reviews. Cancer (2013-05-11)
Philip J Hogg

Protein action in nature is generally controlled by the amount of protein produced and by chemical modification of the protein, and both are often perturbed in cancer. The amino acid side chains and the peptide and disulphide bonds that bind the polypeptide backbone can be post-translationally modified. Post-translational cleavage or the formation of disulphide bonds are now being identified in cancer-related proteins and it is timely to consider how these allosteric bonds could be targeted for new therapies.

Product Number
Product Description

L-Cystine, ≥98% (TLC), crystalline
L-Cystine, from non-animal source, meets EP testing specifications, suitable for cell culture, 98.5-101.0%
L-Cystine, ≥99.7% (TLC)
L-Cystine, PharmaGrade, Ajinomoto, EP, Manufactured under appropriate GMP controls for pharma or biopharmaceutical production, suitable for cell culture
L-Cystine, certified reference material, TraceCERT®
Cystine, European Pharmacopoeia (EP) Reference Standard
L-Cystine, produced by Wacker Chemie AG, Burghausen, Germany, ≥98.5%
L-Cystine, PharmaGrade, meets EP specifications, manufactured under appropriate controls for use as a raw material in pharma or biopharmaceutical production, suitable for cell culture

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon


Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.