IL10 Human

Interleukin-10 Human Recombinant
Cat. No.
BT7813
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. 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-10 Human Recombinant produced in E.coli is a single non-glycosylated polypeptide chains containing 161 amino acids each and having a molecular mass of 18.6kDa.
The IL-10 is purified by proprietary chromatographic techniques.

Product Specs

Introduction

Recombinant Interleukin 10 (IL-10) is a cytokine primarily synthesized by monocytes and, to a lesser extent, lymphocytes. It exhibits diverse effects on immune regulation and inflammation. IL-10 suppresses the expression of Th1 cytokines, MHC class II antigens, and costimulatory molecules on macrophages. Furthermore, it promotes B cell survival, proliferation, and antibody production. IL-10 can inhibit NF-kappa B activity and participates in regulating the JAK-STAT signaling pathway. Studies involving knockout mice suggest that IL-10 plays a critical role as an immunoregulator in the intestinal tract.

Description
Recombinant Human Interleukin-10, produced in E.coli, is a single, non-glycosylated polypeptide chain comprising 161 amino acids per chain. It possesses a molecular weight of 18.6 kDa. The purification of IL-10 is achieved using proprietary chromatographic methods.
Physical Appearance
Sterile, filtered, white, lyophilized (freeze-dried) powder.
Formulation
Lyophilized from a 0.2 µm filtered, concentrated (1 mg/mL) solution in phosphate-buffered saline (PBS) at pH 7.4.
Solubility
Reconstitute the lyophilized Interleukin-10 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 as needed.
Stability
Although lyophilized Interleukin-10 remains stable at room temperature for 3 weeks, it is recommended to store it desiccated at or below -18°C. Once reconstituted, IL-10 should be stored at 4°C for 2-7 days. For long-term storage, freeze at or below -18°C. To enhance stability during long-term storage, adding a carrier protein (0.1% HSA or BSA) is recommended. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 97.0% as determined by: (a) Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis, and (b) Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
Biological Activity
The ED50, determined by dose-dependent co-stimulation of MC/9 cells (in the presence of murine IL-4), was found to be less than 2.0 ng/mL. This corresponds to a specific activity of 5.0 x 105 IU/mg.
Synonyms
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
Source
Escherichia Coli.
Amino Acid Sequence
MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR N.

Product Science Overview

Introduction

Interleukin-10 (IL-10) is a crucial anti-inflammatory cytokine that plays a significant role in regulating immune responses. It is produced by various cell types, including T cells, NK cells, macrophages, and monocytes . Recombinant human IL-10 (rhuIL-10) is a synthetic form of this cytokine, designed to mimic the natural IL-10 produced in the human body.

Biological Properties

IL-10 is known for its ability to inhibit the synthesis of pro-inflammatory cytokines such as IFN-γ, IL-2, IL-3, TNF-α, and GM-CSF, which are produced by cells like macrophages and regulatory T cells . This cytokine also enhances the survival, proliferation, and differentiation of B cells, and can block the activation of cytokine synthesis and several accessory functions of macrophages .

Mechanism of Action

IL-10 initiates signal transduction by binding to a cell surface receptor complex consisting of IL-10 receptor I (IL-10RI) and IL-10 receptor II (IL-10RII) . This binding activates the Janus kinase 1 (Jak1) and tyrosine kinase 2 (Tyk2), leading to the phosphorylation of signal transducer and activator of transcription 3 (Stat3) . The activation of Stat3 is crucial for the anti-inflammatory effects of IL-10, as it regulates the expression of various genes involved in immune responses.

Therapeutic Applications

Recombinant human IL-10 has been explored for its therapeutic potential in various inflammatory and autoimmune diseases. For instance, it has been studied in the treatment of Crohn’s disease, where it was found to induce clinical remission and endoscopic improvement in patients with mild to moderately active disease . However, the therapeutic efficacy of rhuIL-10 can be dose-dependent, with higher doses sometimes being less effective .

Safety and Tolerance

Clinical studies have shown that rhuIL-10 is generally safe and well-tolerated. Adverse effects are typically dose-related, mild to moderate in severity, and reversible . Common side effects include asymptomatic anemia and thrombocytopenia at higher doses . Importantly, no serum accumulation of rhuIL-10 or antibodies against IL-10 were detected after 4 weeks of treatment .

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