IL 15 Rat

Interleukin-15 Rat Recombinant
Cat. No.
BT30858
Source
Escherichia Coli.
Synonyms
IL-15, MGC9721.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
Prospec'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.
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Description

Interleukin-15 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids and having a molecular mass of 13533 Dalton.
The IL-15 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
The cytokine encoded by this gene plays a crucial role in regulating the activation and proliferation of T cells and natural killer cells. Sharing numerous biological activities with interleukin-2, this cytokine binds to common hematopoietin receptor subunits, potentially competing with IL-2 for the same receptor and thereby negatively regulating each other's activity. A balance between this cytokine and IL-2 is known to control the number of CD8+ memory cells. This cytokine triggers the activation of JAK kinases, leading to the phosphorylation and activation of transcription activators such as STAT3, STAT5, and STAT6. Studies on the corresponding mouse cytokine suggest that it might enhance the expression of the apoptosis inhibitor BCL2L1/BCL-x(L), possibly through STAT6-mediated transcriptional activation, thereby preventing apoptosis. Two alternative splicing variants of this gene have been identified, both encoding the same protein.
Description
Recombinant Rat Interleukin-15, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 115 amino acids with a molecular weight of 13,533 Daltons. The purification process of IL-15 involves proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The protein was lyophilized from a solution of 10mM Tris buffer at a pH of 8.5.
Solubility
To reconstitute the lyophilized Interleukin-15, it is recommended to dissolve it in sterile 18MΩ-cm H2O at a concentration of at least 100µg/ml. This solution can then be further diluted in other aqueous solutions.
Stability
Lyophilized Interleukin-15 remains stable at room temperature for up to 3 weeks; however, it is recommended to store it desiccated below -18°C. Once reconstituted, IL-15 should be stored at 4°C for 2-7 days. For long-term storage, freezing below -18°C is advised. To enhance stability during long-term storage, consider adding a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 98.0% as assessed by: (a) RP-HPLC analysis. (b) SDS-PAGE analysis.
Biological Activity
The ED50, determined by the dose-dependent stimulation of CTLL-2 cell proliferation, was found to be less than 10 ng/ml. This corresponds to a specific activity of 100,000 IU/mg.
Synonyms
IL-15, MGC9721.
Source
Escherichia Coli.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Asn-Trp-Ile-Asp.

Product Science Overview

Introduction

Interleukin-15 (IL-15) is a cytokine that plays a crucial role in the immune system by promoting the proliferation and maintenance of natural killer (NK) cells and CD8+ T cells. It is structurally and functionally related to Interleukin-2 (IL-2) and is involved in various immunological responses. Recombinant IL-15, including that derived from rats, is used in research to study its effects and potential therapeutic applications.

Discovery and Structure

IL-15 was discovered in 1994 as a cytokine that induces the proliferation of T cells independently of IL-2. It shares common receptor chains with IL-2, specifically the IL-2/15Rβ (CD122) and γc (CD132) chains. The specificity of IL-15 is conferred by its unique alpha receptor chain, IL-15Rα (CD215), which has a high affinity for IL-15 independently of the β and γc chains .

Biological Functions

IL-15 is a pleiotropic cytokine, meaning it has multiple effects on different cell types. It is essential for the development, survival, and function of NK cells, NKT cells, γδ T lymphocytes, and memory CD8+ T cells. IL-15 is involved in both innate and adaptive immunity, making it a critical component of the immune response .

Mechanism of Action

IL-15 exerts its effects through a complex signaling pathway. It binds to the IL-15Rα chain, which presents IL-15 in trans to cells expressing the IL-2/15Rβ and γc chains. This trans-presentation mechanism is unique to IL-15 and allows it to efficiently stimulate target cells. The binding of IL-15 to its receptor activates several downstream signaling pathways, including the JAK/STAT, PI3K/Akt, and MAPK pathways, leading to the proliferation and activation of immune cells .

Therapeutic Potential

Due to its ability to stimulate the immune system, IL-15 has been investigated for its potential therapeutic applications, particularly in cancer immunotherapy. IL-15 can enhance the cytotoxic activity of NK cells and CD8+ T cells, making it a promising candidate for boosting anti-tumor immunity. However, the clinical use of IL-15 has been limited by its short half-life and the need for sustained exposure to achieve optimal therapeutic effects .

Recombinant IL-15

Recombinant IL-15, including rat-derived IL-15, is produced using genetic engineering techniques. It is used in research to study the biological functions and therapeutic potential of IL-15. Recombinant IL-15 can be administered in various forms, including as a single agent or in combination with other immunotherapeutic agents. Recent studies have focused on developing long-acting forms of IL-15 to overcome the limitations of its short half-life .

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