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Renin is a highly specific aspartyl protease that participates in the body’s renin-angiotensin system (RAS). It cleaves angiotensinogen, which is produced in the liver, to yield angiotensin I. This is further converted into angiotensin II by angiotensin converting enzyme. Angiotensin II has been shown to constrict blood vessels and increase sodium reabsorption in the kidneys, leading to increased blood pressure. The primary structure of renin precursor consists of 406 amino acids with a pre- and a pro-segment carrying 20 and 46 amino acids, respectively. Mature renin contains 340 amino acids and has a predicted mass of ~37 kDa.
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Figure 1. Coomassie stained SDS-PAGE. Lane 1, Molecular weight marker. Lane 2, 1.0µg Human active renin (ENZ-PRT193).
Figure 2. Renin activity using the FRET peptide substrate, Arg-Glu(EDANS)-Ile-His-Pro-Phe-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys (DARBCYL)-Arg. Briefly, a 10µg vial of renin (ENZ-PRT193) was resuspended in 100µl dH2O. The renin protein was diluted to 20µg/ml in 50µl of buffer (25mM MES pH6 and 150mM NaCl). Separately, the renin substrate was diluted to 20µM in a 50µl volume. Both the enzyme and substrate were heated to 37°C for 10 minutes. They were then combined and read kinetically every minute for 10 minutes (using Ex350nm / Em 490nm). Interpolation off a standard curve (calibration standard Fmoc-Glu(EDANS)-OH) was used to calculate the activity of the renin enzyme. The activity was calculated to be > 30pmole/µg/min.
| Regulatory Status |
RUO – Research Use Only |
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Related Products
| Alternative Name | Angiotensin-converting enzyme 1, CD143 |
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| Purity | ≥95% (SDS-PAGE) |
| Source | Produced in NSO cells. |