IL 15 Human

Interleukin-15 Human Recombinant
Cat. No.
BT30812
Source
Escherichia Coli.
Synonyms
IL-15, MGC9721.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis 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.
Shipped with Ice Packs
In Stock

Description

Interleukin-15 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids and having a molecular mass of 12.9kDa.

The IL-15 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
This gene encodes a cytokine that plays a crucial role in regulating the activation and proliferation of T cells and natural killer (NK) cells. This cytokine shares significant biological similarities with interleukin-2 (IL-2), including binding to common hematopoietin receptor subunits. Consequently, they may compete for the same receptor, leading to negative regulation of each other's activity. Maintaining a balance between this cytokine and IL-2 is essential for controlling the number of CD8+ memory cells. Notably, this cytokine triggers the activation of JAK kinases, which in turn phosphorylate and activate transcription factors such as STAT3, STAT5, and STAT6. Studies conducted on mice suggest that this cytokine might enhance the expression of the apoptosis inhibitor BCL2L1/BCL-x(L), potentially through STAT6-mediated transcriptional activation, thereby preventing apoptosis. Interestingly, two alternatively spliced transcript variants of this gene have been identified, both of which encode the same protein.
Description

Recombinant human interleukin-15, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 114 amino acids. It has a molecular mass of 12.9 kDa.

The purification of IL-15 is achieved using proprietary chromatographic techniques.

Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The protein was lyophilized from a phosphate-buffered saline (PBS) solution at a pH of 7.4.
Solubility
To reconstitute the lyophilized Interleukin-15, 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 Interleukin-15 remains stable at room temperature for up to 3 weeks. However, for extended storage, it is recommended to store it in a desiccated state below -18°C. After reconstitution, IL-15 should be stored at 4°C for 2-7 days. For long-term storage, it is advisable to add a carrier protein (0.1% HSA or BSA) and store it below -18°C. Repeated freeze-thaw cycles should be avoided.
Purity
The purity is determined to be greater than 97.0% using the following methods:
(a) Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis.
(b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
Biological Activity

The ED50, determined using a cell proliferation assay with MO7e human megakaryocytic leukemic cells, is in the range of 0.3-2.6 ng/ml. This corresponds to a specific activity greater than 1.5 x 10⁷ U/mg.

Synonyms
IL-15, MGC9721.
Source
Escherichia Coli.
Amino Acid Sequence

NWVNVISDLK KIEDLIQSMH IDATLYTESD VHPSCKVTAM KCFLLELQVI SLESGDASIH DTVENLIILA NNSLSSNGNV TESGCKECEE LEEKNIKEFL QSFVHIVQMF INTS.

Product Science Overview

Discovery and Structure

IL-15 was first identified in 1994 as a cytokine that shares many biological activities with IL-2, but it is produced by a wide variety of cell types, including monocytes, macrophages, and dendritic cells . The human recombinant form of IL-15 (rhIL-15) is a non-glycosylated monomer with a molecular weight of approximately 13 kDa, produced using recombinant DNA technology in E. coli .

Biological Functions

IL-15 is essential for the survival and proliferation of NK cells and memory CD8+ T cells. It promotes the differentiation and activation of these cells, enhancing their cytotoxic activity against infected or malignant cells . IL-15 also plays a role in the homeostasis of T cells and the maintenance of long-term immune memory .

Clinical Applications

The potential of IL-15 in cancer immunotherapy has garnered significant interest. IL-15 agonists have shown promising results in preclinical studies, demonstrating their ability to inhibit tumor growth and prevent metastasis . Recombinant human IL-15 has been evaluated in clinical trials for its efficacy in treating various cancers, including chronic lymphocytic leukemia (CLL) and other lymphoid malignancies .

In a Phase I trial, administration of rhIL-15 as a continuous intravenous infusion was associated with a substantial increase in the number of NK cells, indicating its potential to enhance the efficacy of monoclonal antibody therapies . The combination of rhIL-15 with other immunotherapeutic agents, such as obinutuzumab, is being explored to improve treatment outcomes for patients with relapsed and refractory CLL .

Challenges and Future Directions

Despite its potential, the clinical application of IL-15 faces challenges, including the identification of optimal dosing regimens and the management of potential toxicities . Ongoing research aims to address these challenges and further elucidate the mechanisms by which IL-15 can be harnessed for cancer immunotherapy .

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