Recombinant Mouse Renin-2 (REN2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-03573P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Mouse Renin-2 (REN2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-03573P
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Product Overview

Description Recombinant Mouse Renin-2 (REN2) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P00796
Target Symbol REN2
Synonyms Ren2; Ren-2; Renin-2; EC 3.4.23.15; Angiotensinogenase; Submandibular gland renin) [Cleaved into: Renin-2 heavy chain; Renin-2 light chain]
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His
Target Protein Sequence SSLTDLISPVVLTNYLNSQYYGEIGIGTPPQTFKVIFDTGSANLWVPSTKCSRLYLACGIHSLYESSDSSSYMENGDDFTIHYGSGRVKGFLSQDSVTVGGITVTQTFGEVTELPLIPFMLAQFDGVLGMGFPAQAVGGVTPVFDHILSQGVLKEKVFSVYYNRGPHLLGGEVVLGGSDPEHYQGDFHYVSLSKTDSWQITMKGVSVGSSTLLCEEGCEVVVDTGSSFISAPTSSLKLIMQALGAKEKRLHEYVVSCSQVPTLPDISFNLGGRAYTLSSTDYVLQYPN
Expression Range 64-351aa
Protein Length Partial
Mol. Weight 35.0kDa
Research Area Neuroscience
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Renin is a highly specific endopeptidase, related to pepsin, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney. Its function in the salivary gland is not understood.
Subcellular Location Secreted.
Protein Families Peptidase A1 family
Database References

KEGG: mmu:19702

UniGene: PMID: 25194129

  • Intrapulmonary activation of the angiotensin-converting enzyme type 2/angiotensin 1-7/G-protein-coupled Mas receptor axis attenuates pulmonary hypertension in Ren-2 transgenic rats exposed to chronic hypoxia. PMID: 25194138
  • BP-lowering effect of sEH inhibition in I3C-induced Cyp1a1-Ren-2 transgenic rats. PMID: 25224811
  • Hypertension fails to disrupt white matter integrity in young or aged Fisher (F44) Cyp1a1Ren2 transgenic rats. PMID: 25407269
  • A deficitcin Ang-(1-7) in the brain of hypertensive (mRen2)27 rats maycbe a contributing factor to higher blood pressure and alteredcautonomic balance in this strain. PMID: 22526299
  • Data show that the GPR30 agonist G-1 mitigates the adverse effects of oestrogen loss on LV remodelling and the development of diastolic dysfunction in oophorectomized mRen2 Lew rats. PMID: 22328091
  • Epoxide hydrolase inhibitors displays antihypertensive effects in Ren-2 transgenic rats with inducible malignant hypertension via an improvement of renal function. PMID: 21078594
  • Despite similar reductions in blood pressure and renal ET-1 and ANG II levels aliskiren appears to be more effective than losartan, at the doses used, in reducing albuminuria in heterozygous hypertensive Ren-2 rats. PMID: 20666571
  • The increase in urinary angiotensinogen with estrogen depletion or high salt may be a biomarker for glomerular damage reflecting filtration of the circulating protein in the mRen2 Lewis rat strain. PMID: 20462965
  • Compared treatment with a renin inhibitor vs. an AT1R blocker on renal oxidative stress and associated glomerular structural and functional changes in the transgenic Ren2 rat, which manifests hypertension, albuminuria, and increased tissue RAS activity. PMID: 20007350
  • Androgens contribute not only to the development of hypertension, but even more importantly to end-organ damage in TGR(mREN2)27 rats. PMID: 12397037
  • NO synthesis and/or bioavailability as well as sensitivity of arterial smooth muscle cells to NO are decreased in mREN2 rats. PMID: 12512695
  • The greater blood pressure response to L-NAME in ren-2 transgenic rats suggests that prehypertensive rats exhibit an enhanced NO activity in the systemic vasculature PMID: 15795515
  • Ren-2 and angiotensin II have roles in nephrosclerosis PMID: 16522658
  • increased arterial pressure, reduction of renal haemodynamics, and enhancement of intrarenal Ang II levels in hypertensive Cyp1a1-Ren2 transgenic rats PMID: 17083061
  • Blockade of the renin-angiotensin system but not antihypertensive therapy with atenolol reduces vascular pathology in diabetic Ren-2 retina, suggesting that angiotensin II is a causative factor and therapeutic target in diabetic retinopathy. PMID: 17386351
  • Ovariectomy in the older female mRen2.Lewis rat conveys protection against salt-dependent increase in renal injury. PMID: 17630347
  • Oxidative stress contributes to pulmonary hypertension in the transgenic (mRen2)27 rat. PMID: 18424632
  • Report sex differences in circulating and renal angiotensins of hypertensive mRen(2).Lewis but not normotensive Lewis rats. PMID: 18456730
  • suggests that Ang II causes development and progression of NAFLD in the transgenic Ren2 rat model by increasing hepatic ROS PMID: 18486983
  • Perindopril attenuates tubular hypoxia and inflammation in an experimental model of diabetic nephropathy in transgenic Ren-2 rats. PMID: 18826488
  • Chronic immunoneutralization of brain angiotensin-(1-12) lowers blood pressure in transgenic (mRen2)27 hypertensive rats. PMID: 19403863
  • Dual ACE-inhibition and AT1 receptor antagonism improves ventricular lusitropy without affecting cardiac fibrosis in the congenic mRen2.Lewis rat. PMID: 19531557
  • Found that prorenin and aldosterone alone are not sufficient to induce considerable cardiac fibrosis in the absence of sodium load. PMID: 19749160
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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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