Recombinant Proteins

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REN Human

Renin Human Recombinant

This product consists of the human renin enzyme, produced in a laboratory setting using E. coli bacteria. It encompasses amino acids 67 to 406 of the renin protein sequence, resulting in a single chain of 365 amino acids. With a molecular weight of 39.9 kDa, the recombinant renin protein also includes a 25-amino acid His-tag attached to its N-terminus to aid in purification.
Shipped with Ice Packs
Cat. No.
BT13591
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

REN Human, HEK

Renin Human Recombinant, HEK

Recombinant Human Renin is produced in HEK cells and consists of a single polypeptide chain containing 393 amino acids (Leu24-Arg406). It has a molecular weight of 43.7 kDa, including a 10 amino acid His tag at the C-terminus. The protein is glycosylated, enhancing its stability and solubility.
Shipped with Ice Packs
Cat. No.
BT13792
Source
HEK 293.
Appearance
Sterile, white, lyophilized powder.

REN Human, sf9

Renin Human Recombinant, sf9

This recombinant human Renin protein is produced in Sf9 insect cells using a baculovirus expression system. It is a single, glycosylated polypeptide chain consisting of 391 amino acids (residues 24-406) with a molecular weight of 43.3 kDa. The protein appears as a band around 40-57 kDa on SDS-PAGE due to glycosylation. It is purified using proprietary chromatographic techniques and features an 8-amino acid His-tag at the C-terminus for easy detection and purification.
Shipped with Ice Packs
Cat. No.
BT13835
Source
Sf9, Baculovirus cells.
Appearance
The product is supplied as a clear, sterile-filtered solution.

REN Mouse

Renin Mouse Recombinant

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.
Shipped with Ice Packs
Cat. No.
BT13874
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless, and sterile-filtered solution.
Definition and Classification

Renin, also known as angiotensinogenase, is an aspartic protease enzyme secreted by the kidneys. It plays a crucial role in the renin-angiotensin-aldosterone system (RAAS), which regulates blood pressure, fluid, and electrolyte balance . Renin is classified as an enzyme with the EC number 3.4.23.15 .

Biological Properties

Key Biological Properties: Renin is an enzyme that catalyzes the conversion of angiotensinogen to angiotensin I, a precursor to angiotensin II, which is a potent vasoconstrictor .

Expression Patterns: Renin is primarily expressed in the juxtaglomerular cells of the kidneys . It is also found in other tissues, including the placenta .

Tissue Distribution: Renin is predominantly distributed in the kidneys but can also be detected in the plasma, liver, and other tissues .

Biological Functions

Primary Biological Functions: The main function of renin is to regulate blood pressure and fluid balance through the RAAS . It converts angiotensinogen to angiotensin I, which is then converted to angiotensin II, leading to vasoconstriction and increased blood pressure .

Role in Immune Responses and Pathogen Recognition: While renin’s primary role is in blood pressure regulation, it also has implications in immune responses and inflammation .

Modes of Action

Mechanisms with Other Molecules and Cells: Renin acts by cleaving angiotensinogen, produced by the liver, to form angiotensin I . Angiotensin I is then converted to angiotensin II by angiotensin-converting enzyme (ACE), primarily in the lungs .

Binding Partners and Downstream Signaling Cascades: Angiotensin II binds to AT1 and AT2 receptors, leading to various physiological effects, including vasoconstriction, aldosterone release, and increased sodium reabsorption .

Regulatory Mechanisms

Regulatory Mechanisms: Renin release is regulated by several factors, including blood pressure, sodium levels, and sympathetic nervous system activity . It is inhibited by atrial natriuretic peptide (ANP) and stimulated by prostaglandins and nitric oxide .

Transcriptional Regulation and Post-Translational Modifications: Renin gene expression is regulated at the transcriptional level by various factors, including cAMP and calcium . Post-translational modifications, such as glycosylation, also play a role in renin’s activity .

Applications

Biomedical Research: Renin is a key target in hypertension research. Transgenic mice models have been used to study the effects of renin on blood pressure regulation .

Diagnostic Tools: Renin levels are measured to diagnose and manage conditions like hypertension and heart failure .

Therapeutic Strategies: Renin inhibitors, ACE inhibitors, and angiotensin receptor blockers (ARBs) are used to treat hypertension and related cardiovascular diseases .

Role in the Life Cycle

Development to Aging and Disease: Renin plays a critical role throughout the life cycle. During development, it helps regulate blood pressure and fluid balance. In aging, dysregulation of renin can lead to hypertension and cardiovascular diseases .

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