IL 4 Human, His

Interleukin-4 Human Recombinant, His Tag
Cat. No.
BT5289
Source
Escherichia Coli.
Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
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-4 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 150 amino acids fragment (25-153) and having a total molecular mass of 17.2kDa.
The IL-4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Interleukin-4, a pleiotropic cytokine primarily produced by activated T lymphocytes, basophils, and mast cells, exhibits diverse immune response-modulating functions across various cell types. It plays a crucial role in regulating isotype switching, inducing IgE production in B lymphocytes, and differentiating precursor T helper cells. IL-4 binds to both membrane-bound and soluble forms of the IL-4 receptor.
Description
Recombinant human Interleukin-4, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 150 amino acids (fragment 25-153) with a molecular weight of 17.2 kDa. The IL-4 protein includes a 20 amino acid His-tag at the N-terminus and undergoes purification via proprietary chromatographic methods.
Physical Appearance
A clear, sterile, and filtered solution.
Formulation
Interleukin-4 His-Tag is supplied in a buffer containing 20mM Tris-HCl and 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Biological Activity
The ED50, representing the concentration at which 50% of the maximal effect is observed, is less than 0.5 ng/ml as determined by a cell proliferation assay using TF1 human erythroleukemic cells.
Purity
Purity exceeds 95.0% as determined by SDS-PAGE analysis.
Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MHKCDITLQE IIKTLNSLTE QKTLCTELTV TDIFAASKNT TEKETFCRAA TVLRQFYSHH EKDTRCLGAT AQQFHRHKQL IRFLKRLDRN LWGLAGLNSC PVKEANQSTL ENFLERLKTI MREKYSKCSS.

Product Science Overview

Structure and Production

Recombinant human Interleukin-4 (IL-4) is typically produced in Escherichia coli (E. coli) and is available as a lyophilized powder. The recombinant form of IL-4 is a 14.9 kDa protein containing 129 amino acid residues . The His tag, a sequence of histidine residues, is often added to the recombinant protein to facilitate purification and detection .

Biological Functions

IL-4 has several important biological functions, including:

  • Regulation of Immune Responses: IL-4 is a key regulator of immune responses, particularly in the context of allergic inflammation and asthma .
  • B Cell Activation: It stimulates B cell proliferation and differentiation, leading to the production of immunoglobulins such as IgE and IgG1 .
  • T Cell Differentiation: IL-4 promotes the differentiation of naive T cells into TH2 cells, which are essential for the immune response against extracellular pathogens .
Applications

Recombinant human IL-4 is widely used in research and clinical applications, including:

  • Cell Culture: It is used to study the effects of IL-4 on various cell types, including T cells and B cells .
  • Immunotherapy: IL-4 is being investigated for its potential use in immunotherapy for allergic diseases and asthma .
  • Angiogenesis Inhibition: IL-4 has been shown to inhibit VEGF-induced and βFGF-induced angiogenesis, making it a potential therapeutic target for cancer treatment .

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