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Merck

Targeting allosteric disulphide bonds in cancer.

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

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.

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Sigma-Aldrich
L-Cistina, from non-animal source, meets EP testing specifications, suitable for cell culture, 98.5-101.0%
Sigma-Aldrich
L-Cistina, ≥98% (TLC), crystalline
SAFC
L-Cistina
Sigma-Aldrich
L-Cistina, ≥99.7% (TLC)
Sigma-Aldrich
L-Cistina, produced by Wacker Chemie AG, Burghausen, Germany, ≥98.5%
Supelco
L-Cistina, certified reference material, TraceCERT®, Manufactured by: Sigma-Aldrich Production GmbH, Switzerland
L-Cistina, European Pharmacopoeia (EP) Reference Standard