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About This Item
NACRES:
NA.32
UNSPSC Code:
12352200
Form:
lyophilized powder
Assay:
≥95% (SDS-PAGE)
Biological source:
mouse
Recombinant:
expressed in HEK 293 cells
Mol wt:
calculated mol wt 43.2 kDa, observed mol wt 45-55 kDa by SDS-PAGE (reducing) (Protein migrates due to glycosylation. Leu24 is the predicted N-terminus.)
biological source
mouse
recombinant
expressed in HEK 293 cells
tag
6-His tagged (C-terminus)
assay
≥95% (SDS-PAGE)
form
lyophilized powder
mol wt
calculated mol wt 43.2 kDa, observed mol wt 45-55 kDa by SDS-PAGE (reducing) (Protein migrates due to glycosylation. Leu24 is the predicted N-terminus.)
packaging
pkg of 10 μg
impurities
<1 EU/μg endotoxin (LAL test)
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
mouse ... REN(19701)
General description
Renin, also known as REN and angiotensinogenase, is a circulating enzyme that participates in the body′s renin-angiotensin system (RAS). The gene encoding it is localized on mouse chromosome 1.
Biochem/physiol Actions
Renin plays an essential role in the elevation of arterial blood pressure and increased sodium retention by the kidney. It activates the renin-angiotensin system by cleaving angiotensinogen, produced by the liver, to yield angiotensin I, which is further converted into angiotensin II by angiotensin-converting enzyme (ACE), the angiotensin-converting enzyme primarily within the capillaries of the lungs. Renin is secreted from kidney cells, which are activated via signaling from the macula densa, which responds to the rate of fluid flow through the distal tubule, by decreases in renal perfusion pressure (through stretch receptors in the vascular wall), and by sympathetic nervous stimulation, mainly through β-1 receptor activation. It can bind to ATPase H+ transporting accessory protein 2 (ATP6AP2), which results in a fourfold increase in the conversion of angiotensinogen to angiotensin I over that shown by soluble renin. In addition, it′s binding results in phosphorylation of serine and tyrosine residues of ATP6AP2. The level of renin mRNA appears to be modulated by the binding of hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), β subunit (HADHB), HuR and CP1 to a regulatory region in the 3′ UTR. An over-active renin-angiotension system leads to vasoconstriction and retention of sodium and water. These effects lead to hypertension. Therefore, renin inhibitors can be used for the treatment of hypertension.
Physical form
Lyophilized from 0.22 μm filtered solution in PBS. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.
Preparation Note
Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 μg/mL. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Classical Renin-Angiotensin system in kidney physiology.
Sparks MA
Comprehensive Physiology, 4(3), 1201-1228 (2014)
Regulated expression of the Ren-2 gene in transgenic mice derived from parental strains carrying only the Ren-1 gene.
Tronik D
The Embo Journal, 6(4), 983-987 (1987)
Hsin-Chieh Lin et al.
Food & nutrition research, 61(1), 1391666-1391666 (2017-11-21)
Proteins from tilapia frame and skin can potentially be precursors of antihypertensive peptides according to the result of BIOPEP analyses. The aim was to generate peptides with inhibitory effects against angiotensin-converting enzyme (ACE) and renin from tilapia frame and skin protein
Renin: origin, secretion and synthesis.
Persson PB
The Journal of Physiology, 552(Pt 3), 667-671 (2003)
Yu Fu et al.
International journal of biological macromolecules, 101, 207-213 (2017-03-17)
In this work, the inhibitory effects of potato patatin-derived peptides Trp-Gly (WG) and Pro-Arg-Tyr (PRY) on angiotensin I-converting enzyme (ACE) and renin activities were investigated using kinetics, intrinsic fluorescence and molecular docking. The results indicated that PRY was a more
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