Iodoacétamide

L'iodoacétamide agit comme un réactif d'alkylation des résidus cystéine pour le séquençage des peptides. C'est un inhibiteur irréversible des enzymes présentant une cystéine au niveau de leur site actif. Il réagit beaucoup plus lentement avec les résidus histidine, mais cette activité entraîne l'inhibition de la ribonucléase.

Iodoacetamide has been used:

• to prevent enzymatic disulfide reduction in the protein samples
• to inhibit glyceraldehyde-3-phosphate dehydrogenase effectively blocking ATP production in cell biology research

High quality compound suitable for multiple research applications

2-Iodoacetamide is a thiol-alkylating agent frequently used in peptide mapping for biochemical, cell culture and proteomics research. It functions similarly to iodoacetate, primarily binding covalently with the thiol group of cysteine in proteins, thereby preventing the formation of disulfide bonds. This attribute is crucial for several applications, including 2-D protein electrophoresis to reduce streaking and improve resolution, as an inhibitor of deubiquitinase enzymes (DUBs) and a peptidase inhibitor. It is often employed during sample preparation for de novo peptide sequencing with protein mass spectrometry.

It has specific interactions with cysteine and histidine residues in proteins, affecting enzymes like ribonuclease. While it may react slowly with histidine, its inhibitory properties contribute to the research on proteases, such as cysteine proteases. Iodoacetamide is known for its irreversibility in inhibiting enzymes and its ability to form stable protein derivatives, making it valuable in studying protein structures, protein behavior, and enzyme inhibition.

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Packaged in sealed ampules