Recombinantly produced in HEK cell culture and purified by chelated metal affinity chromatography. Contains a 8X-Histidine tag at C terminus for purification. Fully activatable to renin by catalytic amounts of trypsin. Prorenin is a glycosylated aspartic protease that consists of 2 homologous lobes and is the precursor of renin. Prorenin exhibits a low level of enzymatic activity relative to renin which is generated from prorenin by proteolytic cleavage of the first ~43 amino acids at the N-terminus. This so called prosegment appears to block the full enzymatic potential of the active site (1). Renin activates the renin-angiotensin system by cleaving angiotensinogen, produced by the liver, to yield angiotensin I, which is further converted into angiotensin II by ACE, the angiotensin-converting enzyme primarily within the capillaries of the lungs.
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