Resistin Human, His

Resistin Human Recombinant, His Tag
Cat. No.
BT21281
Source
Escherichia Coli.
Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
Prospec's products are furnished forLABORATORY 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

Resistin Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing a 92 amino acids fragment (17-108) of the mature Human Resistin, having a total molecular mass of 14.23kDa and fused with a 4.5kDa amino-terminal hexahistidine tag.
The Resistin is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Resistin, encoded by the RSTN gene, is a peptide hormone and a member of the cysteine-rich secreted protein family known as the RELM family. It is also referred to as ADSF (Adipose Tissue-Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin, in its prepeptide form, comprises 108 amino acids. Its hydrophobic signal peptide undergoes cleavage prior to secretion. In human blood, resistin exists as a dimeric protein formed by two 92-amino acid polypeptides linked by a disulfide bond at Cys26.
Resistin is implicated as a potential link between obesity and insulin resistance. Studies suggest that mouse resistin, primarily produced and secreted by adipocytes, can decrease insulin sensitivity in skeletal muscle myocytes, hepatocytes, and adipocytes. Steppan et al. proposed that resistin inhibits insulin's ability to stimulate glucose uptake and observed elevated resistin levels in obese mice, which were reduced by fasting and antidiabetic drugs. Conversely, Way et al. reported that resistin expression is significantly suppressed in obesity and upregulated by certain antidiabetic drugs.
Research indicates that mouse resistin levels increase during adipocyte differentiation but may also have an inhibitory effect on adipogenesis. In contrast, human adipogenic differentiation appears to be linked to a downregulation of resistin gene expression.
Description
Recombinant Human Resistin, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of a 92 amino acid fragment (17-108) of the mature Human Resistin and has a total molecular mass of 14.23 kDa. It is fused to a 4.5 kDa amino-terminal hexahistidine tag.
The purification of Resistin is achieved through proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The Resistin protein solution is supplied in a buffer of 20mM Tris-HCl at pH 8.0, 5mM EDTA, and 50% glycerol.
Stability
For use within 2-4 weeks, the entire vial should be stored at 4°C. For longer storage, freeze at -20°C.
Repeated freezing and thawing should be avoided.
Purity
SDS-PAGE analysis indicates a purity greater than 95%.
Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Source
Escherichia Coli.

Product Science Overview

Introduction

Resistin, also known as adipose tissue-specific secretory factor (ADSF) or C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein (XCP1), is a cysteine-rich peptide hormone derived from adipose tissue. In humans, it is encoded by the RETN gene . Resistin has been a subject of extensive research due to its controversial role in obesity, insulin resistance, and inflammation.

Structure

Resistin is a small protein with a molecular weight of approximately 12.5 kDa in humans. It consists of 108 amino acid residues in humans and 114 in mice and rats . The structure of resistin mainly comprises a carboxy-terminal disulfide-rich β-sandwich “head” domain with positive electrostatic surfaces and an amino-terminal α-helical “tail” segment with negative electrostatic potential . The crystal structure reveals a multimeric assembly consisting of hexamer-forming disulfide bonds .

Function

Resistin was initially proposed as a link between obesity and diabetes in mice. In humans, resistin is considered to be a pro-inflammatory molecule expressed in immune cells, playing a regulatory role in many chronic inflammatory diseases, metabolic diseases, infectious diseases, and cancers . It has been shown to have key paracrine roles and has a suggested role in type 2 diabetes. Studies show that in obese, diabetic mice, the levels of serum resistin are increased, which has an antagonistic effect on insulin .

Production Process

Human recombinant resistin is produced in E. coli as a single, non-glycosylated polypeptide chain containing a 92 amino acids fragment (17-108) of the mature human resistin. This recombinant protein is fused with a 4.5 kDa amino-terminal hexahistidine tag (His Tag) and purified by proprietary chromatographic techniques . The His Tag facilitates purification and detection of the protein.

Applications

Resistin has several applications in research and clinical settings. It is used as a biomarker for various diseases, including diabetes, obesity, cardiovascular diseases, and atherosclerosis . Additionally, resistin has been identified as a potential diagnostic biomarker for sepsis, with elevated levels observed in sepsis patients . Its role in modulating immune responses and inflammation makes it a valuable target for developing new therapeutic agents.

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