RNLS Human

Renalase Human Recombinant
Cat. No.
BT26742
Source
E.coli.
Synonyms
Renalase FAD-Dependent Amine Oxidase, Chromosome 10 Open Reading Frame 59, Monoamine Oxidase-C, C10orf59, FLJ11218, Renalase, MAO-C, EC 1.4.-.-.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% 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

RNLS Human Recombinant produced in E. coli is a single polypeptide chain containing 349 amino acids (18-342) and having a molecular mass of 38.8 kDa.
RNLS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Renalase (RNLS), a flavin adenine dinucleotide-dependent amine oxidase secreted by the kidneys, functions as a hormone. It metabolizes circulating catecholamines, playing a crucial role in the sympathetic and parasympathetic nervous systems. Elevated catecholamine levels stimulate RNLS activity, secretion, and synthesis.
Description
Recombinant human RNLS, produced in E. coli, is a single polypeptide chain comprising 349 amino acids (residues 18-342) with a molecular weight of 38.8 kDa. This protein is expressed with a 24-amino acid His-tag at the N-terminus and purified using proprietary chromatographic methods.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The RNLS solution is formulated in 20mM Tris-HCl buffer at pH 8.0, containing 2M Urea and 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended periods, store frozen at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Repeated freezing and thawing should be avoided.
Purity
Purity exceeds 90% as determined by SDS-PAGE analysis.
Synonyms
Renalase FAD-Dependent Amine Oxidase, Chromosome 10 Open Reading Frame 59, Monoamine Oxidase-C, C10orf59, FLJ11218, Renalase, MAO-C, EC 1.4.-.-.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMALLRRQ TSGPLYLAVW DKAEDSGGRM TTACSPHNPQ CTADLGAQYI TCTPHYAKKH QRFYDELLAY GVLRPLSSPI EGMVMKEGDC NFVAPQGISS IIKHYLKESG AEVYFRHRVT QINLRDDKWE VSKQTGSPEQ FDLIVLTMPV PEILQLQGDI TTLISECQRQ QLEAVSYSSR YALGLFYEAG TKIDVPWAGQ YITSNPCIRF VSIDNKKRNI ESSEIGPSLV IHTTVPFGVT YLEHSIEDVQ ELVFQQLENI LPGLPQPIAT KCQKWRHSQV TNAAANCPGQ MTLHHKPFLA CGGDGFTQSN FDGCITSALC VLEALKNYI

Product Science Overview

Structure and Function

Renalase is a 342 amino acid protein with a molecular weight of approximately 38 kDa . It shares partial structural similarity with monoamine oxidases, which are enzymes involved in the breakdown of neurotransmitters . Renalase’s primary function is to oxidize catecholamines, such as dopamine, norepinephrine, and epinephrine, thereby regulating their levels in the blood .

Genetic Variations

Genetic variations in the renalase gene have been linked to various cardiovascular and renal diseases . For instance, a functional missense polymorphism (Glu37Asp) has been associated with an increased risk of cardiometabolic disorders . Research has also identified three transcription factors (Sp1, STAT3, and ZBP89) that positively regulate the expression of the renalase gene . Additionally, two microRNAs (miR-29b and miR-146a) have been found to downregulate renalase expression .

Therapeutic Potential

Renalase has shown promise as a therapeutic target for several conditions. Its hypotensive effect suggests that renalase supplementation could be beneficial for treating hypertension . Conversely, inhibiting renalase signaling may be advantageous for patients with cancerous tumors . However, more research is needed to fully understand the therapeutic applications of renalase .

Recombinant Human Renalase

Recombinant human renalase (rhRen1) has been successfully cloned and expressed in E. coli BL21 (DE3) to enhance protein solubility and activity . This recombinant form has been used to study the enzyme’s activity profiles against NAD(P)H isomers and to explore its potential in engineering applications . The administration of recombinant human renalase has been shown to reduce plasma catecholamine levels and ameliorate ischemic acute kidney injury in animal models .

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