IL 10 Rat

Interleukin-10 Rat Recombinant
Cat. No.
BT30278
Source
Escherichia Coli.
Synonyms
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 97.0% 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. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

IL-10 Recombinant Rat produced in E.coli is a single, glycosylated polypeptide chain containing 160 amino acids and having a molecular mass of 18.6 kDa.
The Interleukin-10 Mouse is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Interleukin 10 (IL-10) is a cytokine with diverse roles in regulating immune responses and inflammation. Primarily produced by monocytes and, to a lesser degree, lymphocytes, IL-10 exerts suppressive effects on the immune system. It inhibits the production of pro-inflammatory cytokines by Th1 cells, decreases the expression of major histocompatibility complex (MHC) class II antigens and co-stimulatory molecules on macrophages, and promotes the survival, proliferation, and antibody production of B cells. Additionally, IL-10 has been found to block the activity of nuclear factor kappa B (NF-κB) and participate in the regulation of the Janus kinase/signal transducer and activator of transcription (JAK-STAT) signaling pathway. Studies involving knockout mice have highlighted the critical role of this cytokine in maintaining immune homeostasis within the intestinal tract.
Description
Recombinant Rat IL-10, produced in E. coli, is a single, glycosylated polypeptide chain comprised of 160 amino acids. It exhibits a molecular weight of 18.6 kDa. The purification process of this interleukin-10 mouse variant involves proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White Lyophilized Powder
Formulation
The protein has undergone a lyophilization process and is supplied in a buffer consisting of 20mM Tris-HCl (pH 8.0) and 100mM NaCl.
Solubility
To reconstitute the lyophilized rat IL-10, 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 as needed.
Stability
Lyophilized rat IL-10 demonstrates stability at room temperature for a period of 3 weeks. However, for long-term storage, it is advisable to store the desiccated product at a temperature below -18°C. Upon reconstitution, recombinant rat IL-10 should be stored at 4°C for a duration of 2-7 days. For extended storage periods, it is recommended to freeze the reconstituted product at -18°C. To enhance stability during storage, the addition of a carrier protein (0.1% HSA or BSA) is advised. It is crucial to avoid repeated freeze-thaw cycles to preserve protein integrity.
Purity
The purity of this product exceeds 97.0%, as determined by the following methods: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Biological Activity
The ED50, determined through the dose-dependent inhibition of MC/9 cell proliferation, is less than 10 ng/ml. This corresponds to a Specific Activity of 100,000 IU/mg.
Synonyms
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
Source
Escherichia Coli.
Amino Acid Sequence
SKGHSIRGDN NCTHFPVSQT HMLRELRAAF SQVKTFFQKK DQLDNILLTD SLLQDFKGYL GCQALSEMIK FYLVEVMPQA ENHGPEIKEH LNSLGEKLKT LWIQLRRCHR FLPCENKSKA VEQVKNDFNK LQDKGVYKAM NEFDIFINCI EAYVTLKMKN.

Product Science Overview

Introduction

Interleukin-10 (IL-10) is a cytokine with potent anti-inflammatory properties. It plays a crucial role in regulating the immune response, ensuring that the body does not overreact to pathogens or cause excessive tissue damage. IL-10 is produced by various cell types, including T cells, B cells, macrophages, and dendritic cells. The recombinant form of IL-10, specifically from rats, has been extensively studied for its biological activities and therapeutic potential.

Discovery and Structure

IL-10 was first discovered in 1989 as a cytokine synthesis inhibitory factor produced by T helper 2 (Th2) cell clones . The rat homologue of IL-10 shares approximately 73% identity with human IL-10 at the amino acid sequence level . The active form of IL-10 is a non-covalent homodimer, which means it consists of two identical subunits. In rats, IL-10 has an additional unpaired cysteine residue (cys-149) compared to human IL-10 .

Production and Characterization

Recombinant rat IL-10 is typically produced using bacterial expression systems. The process involves solubilizing and refolding the protein in a glutathione redox system. This method ensures that the protein adopts its active conformation. However, the presence of the unpaired cysteine residue can lead to the formation of disulfide dimers or mixed disulfides with glutathione, reducing the protein’s activity . To overcome this, site-directed mutagenesis is used to replace the cysteine residue with tyrosine, resulting in a more stable and active form of the protein .

Biological Functions

IL-10 is a key anti-inflammatory mediator that helps protect the host from excessive immune responses. It inhibits the production of pro-inflammatory cytokines by myeloid cells and promotes the survival and proliferation of B cells. Additionally, IL-10 has non-classical roles, such as regulating neural and adipose cell processes, promoting CD8 T cell activation, and aiding in epithelial repair .

Therapeutic Potential

The therapeutic potential of IL-10 has been explored in various disease contexts, including autoimmune diseases, cancer, and wound healing. Its ability to modulate the immune response makes it a promising candidate for treating conditions characterized by excessive inflammation . However, the clinical application of IL-10 requires further research to fully understand its mechanisms and optimize its use in different settings.

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