Resistin Rat

Resistin Rat Recombinant
Cat. No.
BT21596
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 White lyophilized (freeze-dried) powder.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis 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

Resistin Rat Recombinant produced in E.Coli is disulfide-linked homodimer consisting of 2x95 amino acid polypeptide chains and having a molecular mass of approximately 20.2kDa.
Resistin is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Resistin, encoded by the RSTN gene, is a peptide hormone classified as a cysteine-rich secreted protein. This family, known as RELM, features proteins with 11 cysteine residues. Resistin is also referred to as ADSF (Adipose Tissue-Specific Secretory Factor) or FIZZ3 (Found in Inflammatory Zone 3). It is believed to play a role in obesity. In mice, resistin is primarily produced and released by adipocytes, acting on skeletal muscle, liver cells, and fat cells to decrease their sensitivity to insulin. Steppan et al. suggest that resistin hinders glucose uptake stimulation and is found at elevated levels in obese mice. Conversely, fasting and antidiabetic medication lower its levels. However, Way et al. observed significantly reduced resistin expression in obesity. Further studies indicate that while resistin increases during adipocyte differentiation, it may also inhibit this process. In humans, adipogenic differentiation likely correlates with reduced resistin gene expression.
Description
Recombinant Rat Resistin, produced in E. coli, is a disulfide-linked homodimer. It comprises two polypeptide chains, each containing 95 amino acids, resulting in a molecular weight of approximately 20.2 kDa. The purification process involves proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
Lyophilized from a 0.2µm filtered solution in PBS with a pH of 7.4 and containing 0.02% Tween-20.
Solubility
To reconstitute the lyophilized Resistin, it is recommended to dissolve it in sterile PBS at a concentration of at least 100µg/ml. This solution can then be diluted further using other aqueous solutions.
Stability
Lyophilized Resistin remains stable at room temperature for up to 3 weeks; however, it should be stored desiccated at a temperature below -18°C for long-term storage. After reconstitution, store Resistin at 4°C for no more than 2-7 days. For extended storage, keep it below -18°C. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 97.0% as determined by: (a) Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) analysis. (b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis.
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.

Amino Acid Sequence

MPSMSLCPMD EAISKKINQD FSSLLPAAMK NTVLHCWSVS SRGRLASCPE GTTVTSCSCG SGCGSWDVRE DTMCHCQCGS IDWTAARCCT LRVGS.

Product Science Overview

Structure and Expression

Resistin is an 11 kDa or 12.5 kDa secretory protein consisting of 94 and 108 amino acids in mice and humans, respectively . The structure of resistin 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 .

In rodents, resistin is primarily expressed in adipocytes, whereas in humans, it is predominantly expressed in leukocytes . This difference in expression patterns between species has implications for its physiological roles.

Physiological Roles

1. Metabolic Regulation: Resistin was originally proposed as a novel adipocytokine involved in insulin resistance and type 2 diabetes in mice . It decreases insulin sensitivity, contributing to the development of metabolic disorders.

2. Inflammation: In humans, resistin is considered a pro-inflammatory molecule that plays a regulatory role in many chronic inflammatory diseases, metabolic diseases, infectious diseases, and cancers . It increases the production of pro-inflammatory cytokines such as tumor necrosis factor-α (TNF-α) and interleukin (IL)-12 through the regulation of the NF-κB signaling pathway .

3. Immune Modulation: Resistin has been shown to enhance the expansion of regulatory T cells (Tregs) through the modulation of dendritic cells . This suggests that resistin plays a role in the immune response by influencing the activity of immune cells.

4. Host Defense: Recent studies have highlighted resistin’s role as a host defense peptide of innate immunity . It exhibits wide-spectrum antimicrobial activity, modulates immunity, and limits microbial product-induced inflammation .

Research and Therapeutic Potential

The understanding of resistin’s participation in host defense mechanisms is still limited, but ongoing research aims to uncover its biological properties, functions, and related mechanisms . This knowledge could provide new insights into the pleiotropic biological functions of resistin and yield promising strategies for developing new antimicrobial therapeutic agents .

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