IL 33 Human, His

Interleukin-33 Human Recombinant, His Tag
Cat. No.
BT4812
Source
Escherichia Coli.
Synonyms
Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33, IL33.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90.0% 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-33 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 159 amino acids C-terminal fragment (112-270) having a molecular weight of 22.49kDa and fused with a 4.5kDa amino-terminal hexahistidine tag.
The IL-33 His is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Interleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also play a role in regulating gene transcription within producer cells. Structurally similar to IL-1, IL-33 stimulates helper T cells to produce type 2 cytokines. It functions by binding to the IL1RL-1 receptor (also known as ST2), which triggers the activation of NF-kappa-B and MAP kinases. This activation leads to the production of cytokines by Th2 cells in vitro. In vivo, IL-33 induces the expression of IL-4, IL-5, and IL-13, resulting in significant pathological changes in mucosal organs. Furthermore, in vitro studies demonstrate that caspase-1 can cleave IL-33 into a 12kDa N-terminal fragment and an 18kDa C-terminal fragment.
Description
Recombinant Human Interleukin-33, produced in E. coli, is a non-glycosylated polypeptide chain consisting of 159 amino acids. This C-terminal fragment (112-270) has a molecular weight of 22.49kDa and includes a 4.5kDa amino-terminal hexahistidine tag. The purification of IL-33 His is achieved through proprietary chromatographic techniques.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
The Interleukin-33 protein solution is provided in a buffer consisting of 10mM Tris-HCl (pH 8.0), 180mM NaCl, and 50% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. Repeated freezing and thawing should be avoided.
Purity
The purity of the product is greater than 90.0%, as determined by SDS-PAGE analysis.
Synonyms
Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33, IL33.
Source
Escherichia Coli.

Product Science Overview

Introduction

Interleukin-33 (IL-33) is a cytokine belonging to the IL-1 family, known for its role in immune response modulation. The recombinant form of IL-33, tagged with a histidine (His) tag, is widely used in research to study its biological functions and interactions.

Structure and Expression

IL-33 is a 32 kDa proinflammatory cytokine composed of 169 amino acid residues . It is primarily expressed in endothelial cells, epithelial cells, fibroblasts, and mesenchymal cells . The recombinant IL-33 is often produced in Escherichia coli expression systems and tagged with a His tag at the C-terminus to facilitate purification and detection .

Biological Functions

IL-33 plays a crucial role in the immune system by binding to its receptor, ST2 (IL1RL1), and activating downstream signaling pathways such as NF-κB and MAPK . This activation leads to the production of type 2 cytokines, including IL-5 and IL-13, which are essential for allergic inflammation and immune response .

Mechanism of Action

Upon binding to the ST2 receptor, IL-33 activates various immune cells, including mast cells, basophils, eosinophils, and natural killer cells . It acts as a chemoattractant for Th2 cells and may function as an “alarmin,” amplifying immune responses during tissue injury . Proteolytic processing by enzymes such as cathepsin G and neutrophil elastase produces more active C-terminal peptides .

Applications in Research

Recombinant IL-33 with a His tag is used in various research applications, including:

  • sELISA (sandwich ELISA): To quantify IL-33 levels in biological samples .
  • SDS-PAGE: To analyze the purity and molecular weight of IL-33 .
  • Functional assays: To study the biological activity of IL-33 in inducing cytokine production and cell proliferation .
Storage and Stability

The recombinant IL-33 protein is typically lyophilized and stored at -20°C or lower for long-term stability . Upon reconstitution, it should be stored under sterile conditions to prevent degradation and maintain its biological activity .

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