IL 2 Mouse

Interleukin-2 Mouse Recombinant
Cat. No.
BT1977
Source
Escherichia Coli.
Synonyms

Interleukin-2, 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 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids and having a molecular mass of 17.2kDa.
The IL-2 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Interleukin 2 (IL-2) is a cytokine that plays a crucial role in the immune system, particularly in the proliferation and differentiation of T cells. It is produced by activated T cells and acts as a growth factor for both T cells and B cells. IL-2 exerts its effects by binding to a specific receptor complex on the surface of immune cells.
Description
Recombinant Mouse Interleukin-2 is a non-glycosylated protein produced in E. coli. It consists of a single polypeptide chain containing 148 amino acids, with a molecular weight of approximately 17.2 kDa. The protein is purified using proprietary chromatographic techniques to ensure high purity.
Physical Appearance
White, lyophilized (freeze-dried) powder that is sterile and has been filtered.
Formulation
The lyophilized Mouse IL-2 is provided as a concentrated solution (1 mg/ml) in 20 mM phosphate-buffered saline (PBS) at pH 7.4, which has been sterile-filtered through a 0.2 µm filter.
Solubility
To reconstitute the lyophilized Mouse IL-2, it is recommended to dissolve it in sterile, deionized water (18 MΩ-cm resistivity) at a concentration of at least 100 µg/ml. The reconstituted solution can be further diluted in other aqueous solutions as needed.
Stability
Lyophilized Interleukin-2 remains stable at room temperature for up to 3 weeks; however, it is recommended to store it in a desiccated state at -18°C or lower for optimal long-term storage. After reconstitution, the IL-2 solution can be stored at 4°C for 2-7 days. For extended storage, it is advisable to freeze the solution at -18°C or lower. To prevent protein degradation, it is best to avoid repeated freeze-thaw cycles. Adding a carrier protein such as albumin (HSA or BSA) at a concentration of 0.1% can help improve stability during storage.
Purity
The purity of the protein is determined using two methods: reverse-phase high-performance liquid chromatography (RP-HPLC) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The results from both analyses indicate a purity greater than 97%.
Biological Activity
The biological activity of the recombinant Mouse IL-2 is measured by its ability to stimulate the proliferation of murine CTLL-2 cells, a cell line that is dependent on IL-2 for growth. The ED50, which represents the concentration of IL-2 required to achieve half-maximal stimulation, is determined to be less than 0.2 ng/ml. This corresponds to a specific activity of 5 x 106 IU/mg.
Protein Content
The protein content of the recombinant Mouse IL-2 is quantified using two independent methods: ultraviolet (UV) spectroscopy and RP-HPLC analysis. UV spectroscopy is performed at a wavelength of 280 nm, using an extinction coefficient of 0.482 for a 0.1% (1 mg/ml) solution, which is calculated based on the amino acid sequence of the protein. RP-HPLC analysis utilizes a calibrated solution of IL-2 as a reference standard for accurate quantification.
Synonyms

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

Source
Escherichia Coli.
Amino Acid Sequence
PTSSSTSSST AEAQQQQQQQ QQQQQHLEQL LMDLQELLSR MENYRNLKLP RMLTFKFYLP KQATELKDLQ CLEDELGPLR HVLDLTQSKS FQLEDAENFI SNIRVTVVKL KGSDNTFECQ FDDESATVVD FLRRWIAFCQ SIISTSPQ.

Product Science Overview

Discovery and Structure

Interleukin-2 was the first interleukin molecule to be discovered. It was purified to homogeneity by immunoaffinity chromatography by Kendall Smith and his team at Dartmouth Medical School . The molecule was also the first cytokine shown to mediate its effects via a specific IL-2 receptor and was the first interleukin to be cloned and expressed from a complementary DNA (cDNA) library .

The recombinant mouse IL-2 protein is typically expressed in Escherichia coli (E. coli) and consists of 150 amino acids with a calculated molecular mass of approximately 17.4 kDa . It is often supplied in a lyophilized form to ensure stability and ease of storage .

Function and Mechanism

IL-2 is best known for its potent stimulatory activity for antigen-activated T cells. It is expressed by various cell types, including CD4+ and CD8+ T cells, gamma delta T cells, B cells, dendritic cells, and eosinophils . Upon binding to its receptor, which consists of CD25, CD122, and CD132, IL-2 activates several signaling pathways, including JAK3-, STAT5-, and AKT-dependent pathways, leading to cellular proliferation and survival .

IL-2 also promotes the peripheral development of regulatory T cells (Tregs), which are essential for maintaining immune tolerance and preventing autoimmune diseases . Additionally, IL-2 is involved in the activation and proliferation of natural killer (NK) cells .

Applications

Recombinant mouse IL-2 is widely used in research to study immune responses and to develop immunotherapies. It is used in cell proliferation assays, where its activity is measured by its ability to stimulate the proliferation of CTLL-2 mouse cytotoxic T cells . The recombinant protein is also used in functional ELISA assays to study its binding to IL-2 receptors .

Stability and Storage

Recombinant mouse IL-2 is typically lyophilized from a sterile solution containing various stabilizers such as trehalose, mannitol, and Tween-80 . It is stable for up to twelve months when stored at -20°C to -80°C under sterile conditions . It is recommended to avoid repeated freeze-thaw cycles to maintain its activity .

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