IL 1 beta Human

Interleukin-1 beta Human Recombinant
Cat. No.
BT29534
Source
Escherichia Coli.
Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis 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-1 beta Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 153 amino acids and having a molecular mass of 17000 Dalton.
The IL-1 Beta is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Interleukin-1 beta (IL-1β) is a cytokine produced by activated macrophages. It plays a crucial role in the immune response by stimulating thymocyte proliferation, inducing IL-2 release, promoting B-cell maturation and proliferation, and enhancing fibroblast growth factor activity. IL-1β is recognized as an endogenous pyrogen, contributing to the inflammatory response, and has been reported to stimulate prostaglandin release from synovial cells.
Description
Recombinant Human Interleukin-1 beta, produced in E. coli, is a non-glycosylated polypeptide chain consisting of 153 amino acids. With a molecular weight of 17 kDa, this purified protein is obtained through proprietary chromatographic techniques.
Physical Appearance
White, lyophilized (freeze-dried) powder, sterile filtered.
Formulation
IL-1 Beta is lyophilized from a sterile solution at a concentration of 1 mg/ml. The solution contains 50 mM Phosphate buffer (pH 7.1) and 150 mM NaCl.
Solubility
To reconstitute the lyophilized Interleukin-1 beta, it is recommended to dissolve it in sterile 18 MΩ-cm H2O at a concentration of at least 100 µg/ml. This solution can be further diluted in other aqueous solutions.
Stability
Lyophilized Interleukin-1 beta remains stable at room temperature for up to 3 weeks; however, it is recommended to store it desiccated below -18°C. Upon reconstitution, IL-1 Beta should be stored at 4°C for 2-7 days. For long-term storage, freezing below -18°C is recommended. To enhance stability during long-term storage, consider adding a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
Purity
The purity of this product is greater than 98.0%, as determined by the following methods: (a) RP-HPLC analysis and (b) SDS-PAGE analysis.
Biological Activity
The specific activity, assessed through a mouse thymus lymphocyte proliferation augmentation assay, is 200,000,000 IU/mg.
Protein Content
Protein quantification was performed using two independent methods: 1. UV spectroscopy at 280 nm, employing an absorbance value of 0.631 as the extinction coefficient for a 0.1% (1 mg/ml) solution. This value is derived from the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. RP-HPLC analysis, utilizing a calibrated solution of Recombinant IL-1 beta as a Reference Standard.
Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Source
Escherichia Coli.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Val-Arg-Ser.

Product Science Overview

Introduction

Interleukin-1 beta (IL-1β) is a proinflammatory cytokine that plays a crucial role in the body’s immune response. It is produced by activated macrophages, monocytes, and dendritic cells in response to inflammatory stimuli . IL-1β is involved in various cellular activities, including cell proliferation, differentiation, and apoptosis .

Structure and Synthesis

IL-1β is initially synthesized as a 31 kDa inactive pro-form that accumulates in the cytosol . The active form of IL-1β is a 17.3 kDa protein containing 153 amino acid residues . The conversion from the inactive to the active form requires the activation of inflammasomes, which are multi-protein complexes that respond to pathogens, stress conditions, and other danger signals . Inflammasome activation triggers the processing of the caspase-1 precursor into its active form, which in turn cleaves pro-IL-1β .

Mechanism of Action

IL-1β lacks a signal sequence peptide for the classical ER/Golgi pathway and is secreted alongside caspase-1 via an alternate and incompletely understood mechanism . Although IL-1β is most often secreted in its active form, secretion of the uncleaved protein may be detectable under some biological conditions .

Biological Functions

IL-1β is an important mediator of the inflammatory response and is involved in a variety of cellular activities . It induces the expression of cyclooxygenase-2 (COX-2) in the central nervous system, contributing to inflammatory pain hypersensitivity . Additionally, IL-1β, in combination with IL-23, induces the expression of IL-17, IL-21, and IL-22 by γδ T cells, suggesting its role in the modulation of autoimmune inflammation .

Applications of Human Recombinant IL-1β

Recombinant human IL-1β is used in various research and clinical applications. It can be used for the maturation of monocyte-derived dendritic cells (Mo-DCs) and for differentiation within the lymphoid lineage, such as Th17 development and B cell proliferation . The proinflammatory cytokine is produced upon infection or injury and is involved in diverse cellular processes .

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