IL 4 Rat

Interleukin-4 Rat Recombinant
Cat. No.
BT5533
Source
Escherichia Coli.
Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity

Greater than 95.0% 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-4 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids and having a molecular mass of 14kDa.
The IL-4 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Interleukin-4 (IL-4) is a cytokine with diverse roles in the immune system. Primarily produced by activated T cells, IL-4 interacts with the interleukin 4 receptor, which also binds IL-13. This shared receptor contributes to the functional overlap between IL-4 and IL-13. IL-4's immune regulatory effects are primarily mediated through STAT6, a transcription factor. The gene encoding IL-4 is located on chromosome 5q, clustered with genes for other cytokines including IL-3, IL-5, IL-13, and CSF2. Notably, IL-4 is in close proximity to IL-13 within this cluster. The expression of IL-4, IL-13, and IL-5 is coordinately regulated by multiple long-range regulatory elements spanning over 120 kilobases on the chromosome. Alternative splicing of the IL-4 gene results in two transcript variants encoding distinct isoforms.
Description
Recombinant Rat Interleukin-4, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 125 amino acids. It has a molecular weight of 14 kDa. The purification of IL-4 is achieved using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder
Formulation
Lyophilized from a 0.2 µm filtered concentrated solution in PBS pH 7.4 and 5% trehalose.
Solubility
Reconstitute the lyophilized Interleukin-4 in sterile 18 MΩ-cm H2O to a concentration of at least 100 µg/ml. This solution can be further diluted in other aqueous solutions.
Stability
Lyophilized Interleukin-4 is stable at room temperature for 3 weeks, but it is recommended to store it desiccated below -18°C. After reconstitution, store IL-4 at 4°C for 2-7 days. For long-term storage, freeze IL-4 below -18°C. It is recommended to add a carrier protein (0.1% HSA or BSA) for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity greater than 95.0% as determined by: (a) RP-HPLC analysis (b) SDS-PAGE analysis
Biological Activity
The ED50, determined using a cell proliferation assay with rat splenocytes, is less than 2 ng/ml, which corresponds to a specific activity of 500,000 IU/mg.
Protein Content
Protein quantification was performed using two independent methods: 1. UV spectroscopy at 280 nm, using an absorbance value of 0.2 as the extinction coefficient for a 0.1% (1 mg/ml) solution. This value is calculated using the PC GENE computer analysis program for protein sequences (IntelliGenetics). 2. RP-HPLC analysis, employing a standard solution of IL-4 as a reference standard.
Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
Source
Escherichia Coli.
Amino Acid Sequence

HGCNDSPLR EIINTLNQVT EKGTPCTEMF VPDVLTATRN TTENELICRA SRVLRKFYFP RDVPPCLKNK SGVLGELRKL CRGVSGLNSL RSCTVNESTL TTLKDFLESL KSILRGKYLQ SCTSMS.

Product Science Overview

Introduction

Interleukin-4 (IL-4) is a pleiotropic cytokine that plays a crucial role in the immune system. It is also known as B cell-stimulatory factor-1 (BSF-1) or B cell growth factor-1 (BCGF-1) . Recombinant IL-4 from rats is often used in research to study its effects and mechanisms in various biological processes.

Structure and Properties

IL-4 is a monomeric glycoprotein with a molecular weight ranging from approximately 13 kDa to 18 kDa . It contains three intrachain disulfide bridges and adopts a bundled four alpha-helix structure . The recombinant form of rat IL-4 is typically produced in E. coli and is a non-glycosylated polypeptide chain containing 125 amino acids .

Biological Functions

IL-4 is primarily produced by activated T cells, mast cells, and bone marrow stromal cells . It induces the differentiation of naive helper T cells (Th0 cells) into Th2 cells, which are essential for humoral immunity . IL-4 also stimulates the proliferation and differentiation of B cells, enhances the expression of MHC class II molecules, and promotes the production of IgE and IgG1 antibodies .

Applications in Research

Recombinant rat IL-4 is widely used in immunological research to study its role in various cellular processes. It is used in cell proliferation assays, where it has been shown to stimulate the proliferation of rat splenocytes . Additionally, IL-4 is used to investigate its effects on macrophages, where it has been observed to increase the expression of Arg1 without affecting iNOS or IL-6 .

Production and Purity

Recombinant rat IL-4 is produced in E. coli and is available in both carrier-free and carrier-containing formulations . The carrier-free version is recommended for applications where the presence of bovine serum albumin (BSA) could interfere with the results . The purity of recombinant rat IL-4 is typically greater than 95% as determined by SDS-PAGE and HPLC . The endotoxin level is less than 1 EU/μg of the protein, as determined by the LAL method .

Storage and Stability

Recombinant rat IL-4 is lyophilized from a 0.2 μm filtered solution in PBS and can be reconstituted in sterile distilled water or aqueous buffer containing 0.1% BSA . It is stable for 12 months when stored at -20 to -70°C as supplied . After reconstitution, it can be stored at 2 to 8°C for one month or at -20 to -70°C for long-term storage . It is important to avoid repeated freeze-thaw cycles to maintain its stability and activity .

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