Cayman PCSK9 (human, recombinant)

Proprotein convertase subtilisin kexin 9 (PCSK9) is a zymogen and member of the subtilisin serine protease family that reduces protein levels of LDL receptors (LDLRs), the receptor for LDL-cholesterol (LDL-C).^, It is primarily expressed in the liver and is composed of an N-terminal prodomain that regulates PCSK9 maturation, a catalytic domain containing a catalytic aspartic acid-histidine-serine triad, and a C-terminal domain that contains the LDLR binding site.^,, PCSK9 is synthesized as a proprotein that is autocatalytically cleaved to generate the 63 kDa mature protein in which the N-terminal prodomain remains non-covalently bound to the catalytic domain to inhibit further activity. The mature PCSK9 is secreted and circulates in the plasma where it binds to cell surface-expressed LDLRs, triggering endocytosis and lysosomal degradation of the PCSK9-LDLR complex. This action decreases LDLR expression and reduces cellular LDL-C uptake. Gain-of-function and loss-of-function PCSK9 mutations have been associated with autosomal dominant hypercholesterolemia and decreased plasma LDL-C levels, respectively, in humans. Reducing the activity of circulating PCSK9 with monoclonal antibodies or small molecule inhibitors decreases LDL-C levels and reduces the risk of adverse cardiovascular events in individuals with hypercholesterolemia. Caymans PCSK9 (human, recombinant) protein is synthesized as a 76 kDa proprotein. After cleavage of the signal peptide PCKS9 autocatalytically cleaves to the ~15 kDa prodomain and the ~60 kDa mature form and can be used for ELISA, flow cytometry (FC), and Western blot (WB) applications.

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