Recombinant Mouse REN1/Renin-1 Protein (His Tag) | PKSM041281

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SKU:
575-PKSM041281
€567.00
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Description

Recombinant Mouse REN1/Renin-1 Protein (His Tag) | PKSM041281 | Gentaur US, UK & Europe Disrtribition

Synonyms: Renin-1; Angiotensinogenase; Kidney renin; Ren1; Ren; Ren-1;Angiotensin-forming enzyme;Ren-A;Ren1c;Ren1d;Rn-1;Rnr

Active Protein: N/A

Activity: Recombinant Mouse Renin is produced by our Mammalian expression system and the target gene encoding Leu22-Arg402 is expressed with a 10His tag at the C-terminus.

Protein Construction: Recombinant Mouse Renin is produced by our Mammalian expression system and the target gene encoding Leu22-Arg402 is expressed with a 10His tag at the C-terminus.

Fusion Tag: C-His

Species: Mouse

Expressed Host: Human Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 43.5 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Reconstitution: Please refer to the printed manual for detailed information.

Background: Mouse Renin, also known as Renin-1, is a member of the peptidase A1 amily. Renin is synthesized by the juxtaglomerular cells of the kidney in response to decreased blood pressure and sodium concentration. It cleaves angiotensinogen to generate angiotensin I, which can be further converted by angiotensin converting enzyme (ACE) to angiotensin II. Angiotensin II is the active molecule of the reninangiotensin system that acts by binding to angiotensin receptors type 1 and 2 (AT1 and AT2), and has direct pathophysiological effects on the heart and peripheral vasculature. After secretion, inactive prorenin can be proteolytically activated by trypsin, cathepsin B, or other proteinases.

Research Area: N/A

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