IL 31 Human

Interleukin-31 Human Recombinant
Cat. No.
BT4347
Source
Escherichia Coli.
Synonyms
Interleukin 31, IL31, IL-31.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

IL-31 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (24-164 a.a.) and having a molecular mass of 15.8 kDa.

Product Specs

Introduction
IL-31, primarily produced by activated Th2-type T cells, interacts with a receptor complex comprising IL-31 Receptor A and Oncostatin-M Receptor, which is consistently present on epithelial cells and keratinocytes. This cytokine plays a significant role in the pathogenesis of allergic skin conditions and the regulation of other allergic responses like asthma. In atopic dermatitis, IL-31 contributes to the sensation of itch and promotes scratching behavior in NC/Nga mice. Its expression is linked to CLA(+) T cells and is involved in the development of skin inflammation and itching associated with atopic dermatitis. Furthermore, IL-31 acts as a potent inducer of proinflammatory mediators in human colonic SEMFs. As a proinflammatory cytokine originating from Th2 cells, IL-31 exhibits elevated serum levels in patients with atopic dermatitis. Its diverse roles extend beyond the immune system, influencing hematopoiesis, immune responses, inflammatory bowel disease, airway hypersensitivity, and dermatitis.
Description
Recombinant human IL-31, produced in E. coli, is a single, non-glycosylated polypeptide chain composed of 141 amino acids (residues 24-164). It has a molecular weight of 15.8 kDa.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
The IL-31 protein (at a concentration of 1mg/ml) was lyophilized using a buffer solution containing 20mM Phosphate, 150mM NaCl at a pH of 7.4.
Solubility
To reconstitute the lyophilized IL-31, it is recommended to dissolve it in sterile 18 megaohm-cm H2O to a concentration of at least 100 micrograms per milliliter. This solution can then be further diluted into other aqueous solutions as needed.
Stability
Lyophilized recombinant IL-31, while stable at room temperature for up to 3 weeks, should ideally be stored in a dry environment below -18 degrees Celsius. Once reconstituted, IL-31 should be stored at 4 degrees Celsius for short-term use (2-7 days). For long-term storage, it should be kept at or below -18 degrees Celsius. Repeated freezing and thawing of the protein should be avoided.
Purity
The purity of this product is greater than 95.0%, as determined by two methods: (a) Size Exclusion-High Performance Liquid Chromatography (SEC-HPLC) analysis and (b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis.
Biological Activity
The ED50, determined by the ability of IL-31 to activate STAT signaling following interaction with its receptor, is less than 5 nanograms per milliliter. This corresponds to a specific activity of 200,000 units.
Synonyms
Interleukin 31, IL31, IL-31.
Source
Escherichia Coli.
Amino Acid Sequence
SHTLPVRLLR PSDDVQKIVE ELQSLSKMLL KDVEEEKGVL VSQNYTLPCL SPDAQPPNNI HSPAIRAYLK TIRQLDNKSV IDEIIEHLDK LIFQDAPETN ISVPTDTHEC KRFILTISQQ FSECMDLALK SLTSGAQQAT T.

Product Science Overview

Structure and Expression

IL-31 is a 24 kDa protein that forms a four-helix bundle structure, characteristic of the alpha-helical cytokine family. The recombinant form of IL-31 can be expressed in various systems, including E. coli and human embryonic kidney (HEK293) cells . The recombinant protein is often purified to a high degree of purity, typically greater than 95%, and is used in various research applications .

Biological Functions

IL-31 plays a significant role in the immune system, particularly in the regulation of inflammatory responses. It is involved in the pathogenesis of several inflammatory disorders, including:

  • Atopic Dermatitis: IL-31 is known to induce itching and inflammation in the skin, contributing to the symptoms of atopic dermatitis .
  • Alopecia: IL-31 has been implicated in hair loss conditions such as alopecia .
  • Airway Hypersensitivity: IL-31 can contribute to airway inflammation and hypersensitivity, which are characteristic of asthma .
  • Inflammatory Bowel Disease: IL-31 is involved in the inflammatory processes of the gastrointestinal tract .
  • Hepatitis B Related Liver Failure: IL-31 has been associated with liver inflammation and damage in hepatitis B infections .
Mechanism of Action

IL-31 exerts its effects by binding to a heterodimeric receptor complex composed of IL-31 receptor alpha (IL-31RA) and oncostatin M receptor (OSMR). This binding activates several downstream signaling pathways, including the JAK-STAT, PI3K-AKT, and MAPK pathways, leading to the production of various inflammatory mediators .

Applications in Research

Recombinant human IL-31 is widely used in research to study its role in various diseases and to develop potential therapeutic interventions. It is used in cell culture experiments to investigate its effects on different cell types, such as epithelial cells and immune cells . Additionally, IL-31 is used in animal models to study its role in disease pathogenesis and to evaluate the efficacy of potential therapeutic agents .

Production and Purification

Recombinant IL-31 is produced using various expression systems, including E. coli and HEK293 cells. The protein is typically purified using affinity chromatography and other purification techniques to achieve high purity levels. The purified protein is then lyophilized and stored under specific conditions to maintain its stability and bioactivity .

In conclusion, Interleukin-31 (Human Recombinant) is a crucial cytokine involved in various inflammatory processes. Its recombinant form is an essential tool in research, providing insights into its role in disease and aiding in the development of potential therapeutic interventions.

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