IL 33 Human, His

Interleukin-33 Human Recombinant, His Tag
Shipped with Ice Packs
In Stock
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.
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Description

Production and Purification

IL-33 Human, His is synthesized in E. coli and purified via proprietary chromatographic techniques . Key steps include:

  1. Cultivation: High-density fermentation of engineered E. coli strains.

  2. Solubilization: Extraction under denaturing conditions.

  3. Affinity Chromatography: Nickel-based resin captures the His tag.

  4. Refolding: Stepwise dialysis to restore native conformation.

Immunological Activity

  • ST2 Activation: Induces NF-κB and MAPK signaling in Th2 cells and mast cells .

  • Cytokine Induction: Triggers IL-8 secretion in endothelial cells (HUVECs) at nanogram concentrations .

Research Applications

IL-33 Human, His is utilized in:

ApplicationKey Findings
Receptor Binding AssaysValidated for ST2 interaction studies (K<sub>D</sub> = 1.31 nM)
In Vitro BioassaysUsed to model IL-33-driven type 2 inflammation in mast cells and ILC2s
Therapeutic DevelopmentTested in preclinical models of Alzheimer’s disease and asthma
Structural StudiesNMR and X-ray scattering analyses of IL-33/ST2 complexes

Comparative Insights

  • Native vs. Recombinant IL-33: The recombinant protein lacks post-translational modifications (e.g., glycosylation) but retains bioactivity comparable to native IL-33 .

  • Oxidation Sensitivity: Unlike endogenous IL-33, the recombinant form is stabilized against oxidation-induced inactivation .

Key Challenges and Future Directions

  • Limitations: Short half-life in vivo due to rapid oxidation .

  • Innovations: Engineering protease-resistant variants to enhance stability .

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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