IL 17 Human

Interleukin-17 Human Recombinant
Cat. No.
BT30967
Source
Escherichia Coli.
Synonyms
CTLA-8, IL-17, IL-17A, Cytotoxic T-lymphocyte-associated antigen 8.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% 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

Interleukin-17A Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing a total of 264 amino acids (2 chains of 132 aa) and having a molecular mass of 31kDa. 
The IL-17 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
IL-17, also known as interleukin-17A, is a signaling protein that plays a role in immune responses, particularly in the context of inflammation. It is produced by a subset of T helper cells called Th17 cells, as well as other immune cells. IL-17 acts on various cell types, including epithelial cells, fibroblasts, and immune cells, to promote the production of inflammatory mediators such as cytokines, chemokines, and matrix metalloproteinases. These mediators contribute to the recruitment of immune cells to the site of inflammation and the development of inflammatory responses. Dysregulation of IL-17 signaling has been implicated in the pathogenesis of various autoimmune and inflammatory diseases, making it a target for therapeutic intervention in conditions such as rheumatoid arthritis, psoriasis, and inflammatory bowel disease.
Description
Recombinant human interleukin-17A, expressed in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of approximately 31 kDa. It comprises two identical subunits, each containing 132 amino acids, forming a homodimeric structure. The purification process involves proprietary chromatographic techniques to ensure high purity. This product is intended for research purposes only.
Physical Appearance
Sterile, white, lyophilized (freeze-dried) powder.
Formulation
Provided as a sterile, lyophilized powder in a buffer composed of 20 mM citrate, 0.1 M NaCl, at pH 4.5.
Solubility
To reconstitute, it is recommended to dissolve the lyophilized interleukin-17A in sterile, 18 MΩ-cm H2O to a concentration of at least 100 µg/ml. This solution can be further diluted in other aqueous solutions as needed.
Stability
Lyophilized interleukin-17A, when stored desiccated at or below -18°C, is stable for 3 weeks at room temperature. Once reconstituted, it should be stored at 4°C for up to 7 days. For long-term storage, it is advisable to add a carrier protein, such as 0.1% HSA or BSA, and store at or below -18°C. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 95.0% as assessed by SDS-PAGE.
Biological Activity
The biological activity, as measured by the dose-dependent induction of IL-6 in the Hs68 cell line, exhibits an ED50 of approximately 2 ng/ml, corresponding to a specific activity of 500,000 IU/mg.
Protein Content
Protein quantification was conducted using two independent methods: 1. UV spectroscopy at 280 nm, utilizing an absorbance value of 1.13 as the extinction coefficient for a 0.1% (1 mg/ml) solution, calculated using the PC GENE computer analysis program (IntelliGenetics). 2. Analysis by RP-HPLC, employing a standard solution of IL-17 as a reference standard.
Synonyms
CTLA-8, IL-17, IL-17A, Cytotoxic T-lymphocyte-associated antigen 8.
Source
Escherichia Coli.

Product Science Overview

Introduction

Interleukin-17 (IL-17) is a family of pro-inflammatory cytokines that play a crucial role in the immune response. The IL-17 family consists of six members: IL-17A, IL-17B, IL-17C, IL-17D, IL-17E (also known as IL-25), and IL-17F . These cytokines are produced by a subset of T helper cells known as Th17 cells, which are stimulated by IL-23 .

Discovery and Structure

IL-17A, the first member of the IL-17 family, was discovered in 1993 by Rouvier et al., who isolated the IL-17A transcript from a rodent T-cell hybridoma . The protein encoded by IL-17A exhibits high homology with a viral IL-17-like protein found in the genome of Herpesvirus saimiri . The IL-17 family members share a conserved cysteine-rich region, which is crucial for their structure and function .

Biological Functions

IL-17 cytokines are key players in the immune response, particularly in promoting inflammation. They act by binding to their respective receptors, which include IL-17RA, IL-17RB, and IL-17RC . Upon binding, IL-17 activates several signaling cascades that lead to the induction of chemokines. These chemokines recruit immune cells, such as monocytes and neutrophils, to the site of inflammation . IL-17 works in concert with other cytokines, such as tumor necrosis factor (TNF) and interleukin-1 (IL-1), to amplify the inflammatory response .

Clinical Significance

IL-17A is recognized as a hallmark molecule of Th17 cells and plays a pivotal role in various infectious diseases, inflammatory and autoimmune disorders, and cancer . Recent studies have indicated that IL-17A is a biomarker and a therapeutic target in sepsis . Dysregulated expression of IL-17 has been associated with several autoimmune disorders, such as psoriasis .

Recombinant IL-17

Recombinant IL-17 refers to the IL-17 protein that is produced using recombinant DNA technology. This technology allows for the production of large quantities of IL-17 for research and therapeutic purposes. Recombinant IL-17 is used in various studies to understand its role in the immune response and to develop potential therapies for diseases associated with IL-17 dysregulation .

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