https://www.selleckchem.com/pr....oducts/tj-m2010-5.ht
The cell permeable crosslinker divinyl sulfone (DVSF) is active only in the presence of nucleophilic cysteines in proteins and, therefore, traps Trx domains with their substrates, as they form mixed disulfide bonds during the course of their catalytic activity. This allows the identification of substrates that rely on Trx activity for their folding, as well as discovering small molecules that interfere with Trx domain activity. Graphic abstract Identification of thioredoxin domain substrates via divinylsulfone crosslinking and immuno
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