Proteases inhibitors inhibit the proteolytic cleavage of proteins, and they are generally grouped into five major types: cysteine, serine, threonine, aspartate, and metalloproteinase, according to the amino acid active site responsible for proteolytic cleavage. Protease inhibitor cocktails are routinely added to clinical samples used for proteomic studies to inactivate proteases. 1X stock solution contains 500uM AEBSF.HCl, 150 nM aprotinin, 1uM E-64 and 1uM leupeptin hemisulfate.
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