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.

MATERIALS
Product Number
Brand
Product Description

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

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