IL 2 Human

Interleukin-2 Human Recombinant
Cat. No.
BT1704
Source
Escherichia Coli.
Synonyms

T-cell growth factor (TCGF), Lymphokine, IL-2.

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-2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15.4kDa.

The IL-2 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Interleukin 2 (IL2) is a cytokine crucial for the growth and differentiation of T and B lymphocytes, key players in the immune system. The IL2 receptor, a heterotrimeric protein complex, shares its gamma chain with the receptors for IL4 and IL7, highlighting a potential for interconnected signaling pathways. Interestingly, the IL2 gene exhibits monoallelic expression in mature thymocytes, a unique regulatory mechanism for precise gene expression control. Underscoring its importance in immune responses, disruption of a similar gene in mice results in an inflammatory bowel disease resembling ulcerative colitis.
Description
Recombinant Human Interleukin-2, produced in E.Coli, is a single, non-glycosylated polypeptide chain composed of 133 amino acids, with a molecular weight of 15.4kDa. This protein has been purified using proprietary chromatographic techniques to ensure its high quality.
Physical Appearance
White, lyophilized (freeze-dried) powder, sterile.
Formulation
The protein was subjected to sterile filtration using a 0.2 µm filter, concentrated to 1.0 mg/ml in phosphate-buffered saline (PBS) at pH 5.0, and then lyophilized.
Solubility
For reconstitution, dissolve the lyophilized Interleukin-2 in sterile distilled water at a concentration of at least 100 µg/ml. This solution can be further diluted as needed using other aqueous solutions.
Stability
Lyophilized Interleukin-2 remains stable at room temperature for up to 3 weeks; however, it is recommended to store it desiccated at temperatures below -18°C. After reconstitution, IL2 should be stored at 4°C for a period of 2-7 days. For extended storage, freezing at -18°C is recommended. To enhance long-term stability during storage, consider adding a carrier protein like HSA or BSA (0.1%). Minimize freeze-thaw cycles to preserve protein integrity.
Purity
The purity of this product is greater than 97.0%, as determined by two methods: Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) and Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE).
Biological Activity
The biological activity, measured as ED50, represents the concentration required to achieve 50% of the maximum response in a dose-dependent stimulation assay. For this product, the ED50, determined using murine CTLL-2 cells, is less than 0.1 ng/ml. This corresponds to a specific activity of 1 x 107 IU/mg.
Synonyms

T-cell growth factor (TCGF), Lymphokine, IL-2.

Source
Escherichia Coli.
Amino Acid Sequence

APTSSSTKK TQLQLEHLLL DLQMILNGIN NYKNPKLTRM LTFKFYMPKK ATELKHLQCL EEELKPLEEV LNLAQSKNFH LRPRDLISNI NVIVLELKGS ETTFMCEYAD ETATIVEFLN RWITFCQSII STLT.

Product Science Overview

Structure and Source

Recombinant human IL-2 is a 15.5 kDa protein consisting of 134 amino acid residues, including one intrachain disulfide bond . It is typically produced in Escherichia coli (E. coli) for research and therapeutic purposes .

Functions and Mechanisms

IL-2 is best known for its role in inducing the proliferation of T-cells and natural killer (NK) cells . It also stimulates the growth and differentiation of B cells, lymphokine-activated killer cells, monocytes, macrophages, and oligodendrocytes . Additionally, IL-2 promotes the peripheral development of regulatory T cells (Treg cells), which are essential for maintaining immune tolerance .

The effects of IL-2 are mediated through a trimeric receptor complex consisting of IL-2Rα, IL-2Rβ, and the common gamma chain (γc) . Binding of IL-2 to its receptor initiates signaling cascades involving Jak1, Jak3, Stat5, and the PI3K/Akt pathways .

Clinical Applications

Recombinant human IL-2 has been used in various clinical settings, particularly in cancer immunotherapy. It has been employed to boost the immune response in patients with metastatic melanoma and renal cell carcinoma . The ability of IL-2 to activate and expand T-cells and NK cells makes it a valuable tool in adoptive cell transfer therapies.

Research and Development

IL-2 continues to be a subject of extensive research, with ongoing studies exploring its potential in treating autoimmune diseases, enhancing vaccine efficacy, and improving the outcomes of immunotherapy . Researchers are also investigating ways to modify IL-2 to reduce its toxicity and enhance its therapeutic benefits.

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