IL 17 Human, His

Interleukin-17 Human Recombinant, His Tag
Cat. No.
BT30985
Source
Escherichia Coli.
Synonyms
CTLA-8, IL-17, IL-17A, Cytotoxic T-lymphocyte-associated antigen 8, IL17A.
Appearance
Sterile Filtered clear solution.
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 single, non-glycosylated, Polypeptide chain containing 132 amino acids fragment (24-155) having a molecular weight of 19.62kDa and fused with a 4.5kDa amino-terminal hexahistidine tag.
The IL-17A His is purified by proprietary chromatographic techniques.

Product Specs

Introduction
IL-17, a pro-inflammatory cytokine, is secreted by activated T cells. It plays a role in regulating NF-kappaB and mitogen-activated protein kinases. This interleukin stimulates the production of IL-6, cyclooxygenase-2 (COX-2), and nitric oxide (NO). Elevated IL-17 levels are linked to chronic inflammatory conditions such as rheumatoid arthritis, psoriasis, and multiple sclerosis.
Description
Recombinant Human Interleukin-17A, produced in E. coli, is a non-glycosylated polypeptide chain consisting of 132 amino acids (fragment 24-155). With a molecular weight of 19.62 kDa, it includes a 4.5 kDa amino-terminal hexahistidine tag. Purification of IL-17A His is achieved through proprietary chromatographic techniques.
Physical Appearance
A clear solution that has undergone sterile filtration.
Formulation
The Interleukin-17 protein solution (0.171 mg/ml) is provided in a buffer of 25 mM sodium acetate (pH 4.8) and 50% glycerol.
Stability
For optimal storage, refrigerate at 4°C if the entire vial will be used within 2-4 weeks. For extended storage, freeze at -20°C. Repeated freezing and thawing should be avoided.
Purity
SDS-PAGE analysis indicates a purity exceeding 95.0%.
Synonyms
CTLA-8, IL-17, IL-17A, Cytotoxic T-lymphocyte-associated antigen 8, IL17A.
Source
Escherichia Coli.

Product Science Overview

Introduction

Interleukin-17 (IL-17) is a proinflammatory cytokine produced by activated T cells. It plays a crucial role in the immune response by regulating the activities of NF-kappaB and mitogen-activated protein kinases . IL-17 stimulates the expression of other cytokines such as IL-6 and cyclooxygenase-2 (PTGS2/COX-2), and enhances the production of nitric oxide (NO) .

Structure and Production

The human recombinant IL-17 with a His tag is produced in Escherichia coli (E. coli). It is a single, non-glycosylated polypeptide chain containing 132 amino acids, with a molecular weight of approximately 19.62 kDa . The His tag, which is a sequence of histidine residues, is fused to the amino-terminal end of the protein, adding an additional 4.5 kDa to the molecular weight .

Purification and Formulation

The recombinant IL-17 is purified using proprietary chromatographic techniques to achieve a purity greater than 95% as determined by SDS-PAGE . The protein is supplied as a sterile filtered clear solution in 25 mM sodium acetate (pH 4.8) and 50% glycerol . For optimal stability, it should be stored at 4°C if used within 2-4 weeks, or frozen at -20°C for longer periods .

Biological Activity

IL-17 is known for its role in promoting inflammation. It can stimulate the production of other proinflammatory cytokines and chemokines, which recruit immune cells to sites of infection or injury . High levels of IL-17 are associated with several chronic inflammatory diseases, including rheumatoid arthritis, psoriasis, and multiple sclerosis .

Applications

Recombinant IL-17 with a His tag is widely used in laboratory research to study its role in inflammation and immune response. It is also used in assays to screen for potential therapeutic agents that can modulate IL-17 activity .

Safety and Handling

ProSpec’s recombinant IL-17 is intended for laboratory research use only and should not be used as drugs, agricultural or pesticidal products, food additives, or household chemicals . Proper safety protocols should be followed when handling this protein to avoid contamination and ensure accurate experimental results .

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