kallikrein 8

The enzyme is activated by removal of an N-terminal prepropeptide. The highest amidolytic activity is observed using Boc-Val-Pro-Arg┼7-amido-4-methylcoumarin, which is a substrate of α-thrombin. Substrates lacking basic amino acids in the P1 position are not cleaved. The enzyme degrades casein, fibronectin, gelatin, collagen type IV, fibrinogen, and high-molecular-mass kininogen and is associated with diseases such as ovarian cancer and Alzheimer's disease. Belongs in peptidase family S1A.
Supplier Creative Enzymes
Product # EXWM-4113
Pricing 100 ug, contact supplier for pricing
CAS 171715-15-4
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