Human Renin, C-terminal 8x His tag
Recombinantly produced in HEK cell culture and purified by chelated metal affinity chromatography. Contains a 8X-Histidine tag at C terminus for purification. Human renin is produced from the proenzyme prorenin by proteolytic cleavage of a 43 amino acid N-terminal prosegment using limited enzymatic digestion by immobilized trypsin. Conversion to active renin is ~99 percent. 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. 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. It has been reported that the levels of circulating prorenin (but not renin) are increased in diabetic subjects.