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Key Documents

SRP6266

Sigma-Aldrich

Renin from mouse

recombinant, expressed in HEK 293 cells, ≥95% (SDS-PAGE)

Synonym(s):

CYM, CYMP, Chymosin, RENNIN

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

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.

Reconstitution

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Renin: origin, secretion and synthesis.
Persson PB
The Journal of Physiology, 552(Pt 3), 667-671 (2003)
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)
Classical Renin-Angiotensin system in kidney physiology.
Sparks MA
Comprehensive Physiology, 4(3), 1201-1228 (2014)
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
Jeannette Tang et al.
Hypertension (Dallas, Tex. : 1979), 74(1), 83-94 (2019-05-14)
In patients with diabetic kidney disease (DKD), plasma renin activity is usually decreased, but there is limited information on urinary renin and its origin. Urinary renin was evaluated in samples from patients with longstanding type I diabetes mellitus and mice

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