Renin Related Peptides

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CAT# Product Name M.W Molecular Formula Inquiry
R01001 [Cys8] Renin Substrate Tetradecapeptide, rat 1778.1 C83H118N21O21S1 Inquiry
R01002 [Leu8] Renin Substrate Tetradecapeptide, rat 1789.1 C86H125N21O21 Inquiry
R01003 [Val8] Renin Substrate Tetradecapeptide, rat 1775.1 C85H123N21O21 Inquiry
R01007 PHPFHFFVYK 1318.6 C69H87N15O12 Inquiry
R01008 Renin Inhibitor Peptide 1025.2 C52H72N12O10 Inquiry
R01010 H-Pro-His-Pro-Phe-His-Phe-Phe-Val-Tyr-Lys-OH 1318.54 C₆₉H₈₇N₁₅O₁₂ Inquiry
R01011 Z-Arg-Arg-Pro-Phe-His-Sta-Ile-His-Lys(Boc)-OMe 1495.79 C₇₂H₁₁₀N₂₀O₁₅ Inquiry
R01012 H-Leu-Val-Tyr-AMC 550.66 C₃₀H₃₈N₄O₆ Inquiry
R01013 Renin Substrate 1 trifluoroacetate salt 2317.78 C₁₀₉H₁₅₇N₃₁O₂₂S₂ Inquiry
R01015 DABCYL-γ-Abu-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-EDANS trifluoroacetate salt 1798.15 C₉₀H₁₂₀N₂₂O₁₆S Inquiry
R01017 H-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-OH 1645.93 C₇₉H₁₁₆N₂₂O₁₇ Inquiry
R01019 Suc-Arg-Pro-Phe-His-Leu-Leu-Val-Tyr-AMC trifluoroacetate salt 1301.51 C₆₆H₈₈N₁₄O₁₄ Inquiry
R01021 H-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Ser-OH trifluoroacetate salt 1733.01 C₈₂H₁₂₁N₂₃O₁₉ Inquiry
R01022 H-Val-Ile-His-Thr-EDANS acetate salt 716.86 C₃₃H₄₈N₈O₈S Inquiry
R01024 Renin Inhibitor III 1247.6 Inquiry
R01025 Renin 390 FRET Substrate I 2282.7 Inquiry
R01026 Rat Renin Inhibitor Peptide, WFML Peptide 957.3 Inquiry
R01028 Renin Substrate Tetradecapeptide, rat 1823.1 C89H123N21O21 Inquiry
R01031 Angiotensinogen (1-13), human 1645.9 C79H116N22O17 Inquiry

Introduction

Renin Substrates (RS), also known as Angiotensinogen, is a relatively abundant serum globulin in plasma, mainly synthesized in the liver, and is the only known natural renin substrate. After the amino acid fragment is cleaved by renin, a descending peptide precursor, angiotensin I (ATI), is formed. ATI is further converted to a biologically active octapeptide substance, ATII, under the action of angiotensin-converting enzyme. Although RS is not biologically active, its extracellular reserve as an angiotensin peptide may depend on its concentration to limit the rate of transformation of the renin-angiotensin system (RAS) and play an important role in RAS. Therefore, RS plays an important role in the normal development of the cardiovascular system, the maintenance of cardiovascular function, the maintenance of electrolyte and fluid balance, and the regulation of blood pressure.

Mechanism of action

Renin Substrates is hydrolyzed by the action of renin to produce a decapeptide (1-10), which is Ang I. In plasma and tissues, especially in the vascular endothelium of the pulmonary circulation, ACE is present. Under the action of ACE, ATI hydrolyzes 2 amino acid residues by C-terminal hydrolysis to produce an octapeptide (l-8), which is Ang II. In addition, ATI is hydrolyzed by various enzymes to produce a variety of polypeptides. Among them, the role of ATII is the most important. ATII exerts its cardiovascular function mainly through the ATII receptor, which can cause blood vessels to contract and raise blood pressure. Promote the secretion of aldosterone from the adrenal cortex. The action of aldosterone on the renal tubules can play the role of sodium retention, water retention, and potassium release, resulting in increased blood volume.

Application of Renin Substrates

The renin-angiotensin system (RAS) plays an important role in maintaining water and salt balance and regulating cardiovascular activity. Renin Substrates is the only precursor substance of angiotensin, and its concentration changes limit the rate of transformation in RAS. Therefore, controlling RS can prevent cardiovascular diseases such as cerebral infarction.

References

  1. McKinley, M. J., Albiston, A. L., Allen, A. M., Mathai, M. L., May, C. N., McAllen, R. M., ... & Chai, S. Y. (2003). The brain renin–angiotensin system: location and physiological roles. The international journal of biochemistry & cell biology, 35(6), 901-918.
  2. Reynier-Rebuffel, A. M., Pinard, E., Aubineau, P. F., Meric, P., & Seylaz, J. (1983). Generalized cerebral vasoconstriction induced by intracarotid infusion of angiotensin II in the rabbit. Brain research, 269(1), 91-101.
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