IL 32A Human, His

Interleukin-32 alpha Human Recombinant , His Tag
Cat. No.
BT4518
Source
Escherichia Coli.
Synonyms
NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.
Appearance
Sterile filtered colorless 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-32 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids (1-131 a.a.) and having a molecular mass of 19.1 kDa. The IL-32 is fused to a 37 amino acid His Tag at N-terminus and purified by conventional chromatography.

Product Specs

Introduction
IL-32, a member of the cytokine family, plays a critical role in inflammatory responses. It possesses various functional sites, including a tyrosine sulfation site, potential N-myristoylation sites, phosphorylation sites, and an RGD cell-attachment sequence. Elevated IL-32 expression is observed in activated T-cells and NK cells. IL-32 stimulates TNF-a production from macrophages and is involved in the inflammatory response to influenza A virus infection. Dysregulation of IL-32 in myelodysplastic syndrome and chronic myelomonocytic leukemia impacts apoptosis and NK cell function. The p38-MAPK pathway mediates IL-32's induction of TNF, IL-1beta, and IL-6. IL-32 promotes monocyte-to-macrophage differentiation through nonapoptotic, caspase-3-dependent mechanisms. Additionally, IL-32 plays a significant role in the pathogenesis of rheumatoid arthritis and is involved in activation-induced cell death in T cells through intracellular mechanisms. As a cell-associated proinflammatory cytokine, IL-32 is notably stimulated by mycobacteria, leading to the production of interferon gamma via a caspase-1- and IL-18-dependent pathway. Furthermore, IL-32 exhibits associations with TNF-a, IL-1beta, and IL-18, contributing to the development of human rheumatoid arthritis. Targeting IL-32 holds promise for treating autoimmune diseases.
Description
Recombinant human Interleukin-32, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 168 amino acids (with the IL-32 sequence spanning amino acids 1-131). The protein has a molecular weight of 19.1 kDa. For purification purposes, a 37 amino acid His Tag is fused to the N-terminus of IL-32, enabling purification via conventional chromatography techniques.
Physical Appearance
A clear solution, lacking any color, that has been sterilized through filtration.
Formulation
The IL-32 His Tag protein solution is supplied in a buffer containing 20mM Tris-HCl (pH 8), 1mM DTT, and 10% glycerol.
Stability
For optimal storage, the following guidelines are recommended: - If the entire vial will be used within 2-4 weeks, store at 4°C. - For extended storage, freeze at -20°C. - To further enhance long-term stability, consider adding a carrier protein (0.1% HSA or BSA). - Minimize repeated freeze-thaw cycles to maintain protein integrity.
Purity
The purity of this product exceeds 95.0%, as determined by SDS-PAGE analysis.
Synonyms
NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMCF PKVLSDDMKK LKARMHQAIE RFYDKMQNAE SGRGQVMSSL AELEDDFKEGYLETVAAYYE EQHPELTPLL EKERDGLRCR GNRSPVPDVE DPATEEPGES FCDKSYGAPR GDKEELTPQK CSEPQSSK.

Product Science Overview

Structure and Production

The human recombinant IL-32 alpha is produced in Escherichia coli (E. coli) as a single, non-glycosylated polypeptide chain. It contains 168 amino acids, with a molecular mass of approximately 19.1 kDa . The recombinant protein is fused to a 37 amino acid His Tag at the N-terminus, which facilitates its purification through conventional chromatography techniques .

Biological Functions

IL-32 alpha is known for its ability to induce the production of other cytokines such as TNF-alpha, IL-1beta, and IL-6 from macrophages . It activates key cytokine signaling pathways, including NF-kappa-B and p38 MAPK . These pathways are crucial for the inflammatory response and play a role in various immune processes.

Role in Diseases

IL-32 alpha has been implicated in several diseases due to its proinflammatory properties. For instance, it is involved in the pathogenesis of rheumatoid arthritis, where it contributes to the chronic inflammation observed in the disease . Additionally, dysregulation of IL-32 has been noted in conditions such as myelodysplastic syndrome and chronic myelomonocytic leukemia, where it modulates apoptosis and impairs NK cell function .

Applications in Research

The recombinant IL-32 alpha with a His Tag is widely used in laboratory research to study its biological functions and role in diseases. It is particularly useful in experiments requiring high purity and specific activity, such as those investigating cytokine signaling pathways and immune responses .

Storage and Stability

For optimal stability, the IL-32 alpha protein should be stored at 4°C if used within 2-4 weeks. For longer-term storage, it is recommended to keep the protein frozen at -20°C, with the addition of a carrier protein like 0.1% HSA or BSA to prevent degradation . It is important to avoid multiple freeze-thaw cycles to maintain the protein’s integrity.

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