REN Mouse

Renin Mouse Recombinant
Cat. No.
BT13874
Source
Sf9, Baculovirus cells.
Synonyms
Renin-1, Angiotensinogenase, Kidney renin, Ren1, Ren, Ren-A, Ren1c, Ren1d, Rn-1, Rnr.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

REN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 387 amino acids (22-402 a.a.) and having a molecular mass of 42.5kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).
REN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Renin is a highly specific enzyme that plays a crucial role in regulating blood pressure and electrolyte balance. It acts by cleaving angiotensinogen, a protein circulating in the bloodstream, to generate angiotensin I. This process initiates a series of reactions that ultimately lead to an increase in blood pressure and sodium retention by the kidneys.
Description
Recombinant Mouse Renin (REN) is produced in Sf9 insect cells using a baculovirus expression system. This protein is a single, glycosylated polypeptide chain that contains 387 amino acids (amino acids 22-402 of the full-length protein) and has a molecular weight of 42.5 kDa. On SDS-PAGE under reducing conditions, REN migrates between 40-57 kDa due to glycosylation. The protein is expressed with a 6-amino acid Histidine tag at the C-terminus to facilitate purification using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The REN protein is supplied as a solution at a concentration of 0.25 mg/ml in Phosphate Buffered Saline (PBS) with a pH of 7.4 and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), keep the REN protein solution refrigerated at 4°C. For long-term storage, it is recommended to freeze the solution at -20°C. To ensure stability during long-term storage, adding a carrier protein like HSA or BSA to a final concentration of 0.1% is advisable. Avoid repeated freezing and thawing of the protein solution to prevent degradation.
Purity
The purity of the REN protein is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms
Renin-1, Angiotensinogenase, Kidney renin, Ren1, Ren, Ren-A, Ren1c, Ren1d, Rn-1, Rnr.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
LPTRTATFER IPLKKMPSVR EILEERGVDM TRLSAEWGVF TKRPSLTNLT SPVVLTNYLN TQYYGEIGIG TPPQTFKVIF DTGSANLWVP STKCSRLYLA CGIHSLYESS DSSSYMENGS DFTIHYGSGR VKGFLSQDSV TVGGITVTQT FGEVTELPLI PFMLAKFDGV LGMGFPAQAV GGVTPVFDHI LSQGVLKEEV FSVYYNRGSH LLGGEVVLGG SDPQHYQGNF HYVSISKTDS WQITMKGVSV GSSTLLCEEG CAVVVDTGSS FISAPTSSLK LIMQALGAKE KRIEEYVVNC SQVPTLPDIS FDLGGRAYTL SSTDYVLQYP NRRDKLCTLA LHAMDIPPPT GPVWVLGATF IRKFYTEFDR HNNRIGFALA RHHHHHH.

Product Science Overview

Introduction

Renin, also known as REN or angiotensinogenase, is a circulating enzyme that plays a crucial role in the body’s renin-angiotensin system (RAS). This system is essential for regulating blood pressure and fluid balance in the body. The recombinant form of renin from mice is often used in research to study its functions and potential therapeutic applications.

Gene and Expression

The gene encoding renin is localized on mouse chromosome 1. In recombinant studies, renin is typically expressed in HEK 293 cells, which are human embryonic kidney cells. This expression system is chosen because it allows for proper folding and post-translational modifications of the protein, ensuring that the recombinant renin closely mimics the natural enzyme .

Structure and Properties

Renin is a protease enzyme with a calculated molecular weight of approximately 43.2 kDa. However, due to glycosylation, the observed molecular weight can range between 45-55 kDa when analyzed by SDS-PAGE under reducing conditions. The enzyme is often tagged with a 6-His tag at the C-terminus to facilitate purification .

Biological Function

Renin’s primary function is to activate the renin-angiotensin system by cleaving angiotensinogen, a protein produced by the liver, to yield angiotensin I. Angiotensin I is then converted into angiotensin II by the angiotensin-converting enzyme (ACE), primarily within the capillaries of the lungs. Angiotensin II is a potent vasoconstrictor that increases blood pressure and stimulates the release of aldosterone, which promotes sodium retention by the kidneys .

Physiological Role

Renin plays an essential role in the elevation of arterial blood pressure and increased sodium retention by the kidney. It is a key regulator of blood pressure and electrolyte balance, making it a critical target for antihypertensive therapies. Dysregulation of renin activity can lead to conditions such as hypertension and congestive heart failure .

Research and Applications

Recombinant mouse renin is widely used in research to study the mechanisms of blood pressure regulation and to develop new treatments for hypertension and related cardiovascular diseases. It is also used in the development of renin inhibitors, which are a class of antihypertensive drugs that directly inhibit the activity of renin .

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