Peptide Library Construction and Screening
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Sequence | KPSGCGEQNMINFYPNVL |
Functions | Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase. |
Source# | Synthetic |
Solubility | -20°C |
1. C-Peptide replacement therapy and sensory nerve function in type 1 diabetic neuropathy
2. Store-operated Ca2+ entry sustains the fertilization Ca2+ signal in pig eggs
3. Emerging applications of nanotechnology for diagnosis and therapy of disease: a review
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