IL 15 Human, His

Interleukin-15 Human Recombinant, His Tag
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Description

Introduction to IL-15 Human, His

Interleukin-15 (IL-15) Human, His is a recombinant cytokine engineered with a polyhistidine (His) tag for purification and research applications. This protein is a modified version of human IL-15, a pleiotropic cytokine critical for immune regulation, particularly in natural killer (NK) cell development and memory CD8⁺ T-cell homeostasis . The His tag facilitates affinity chromatography-based purification, ensuring high yield and specificity .

Molecular Properties

PropertyDescription
Molecular Weight12.9 kDa (non-glycosylated)
Amino Acid Sequence114 amino acids, including a His tag at the N- or C-terminus
IsoformsDerived from IL-15 SSP (short signal peptide) isoform for cytoplasmic use
Expression SystemEscherichia coli (E. coli)

IL-15 Human, His shares structural homology with IL-2 but binds distinct receptor complexes (IL-15Rα/β/γc) . The His tag does not interfere with receptor binding or biological activity .

Key Production Metrics

ParameterData
Purity>97% (via RP-HPLC and SDS-PAGE)
SolubilityReconstituted in sterile H₂O (≥100 µg/mL)
StabilityStore lyophilized at <-18°C; stable at 4°C for 2–7 days post-reconstitution

IL-15 Human, His is expressed in E. coli, yielding a non-glycosylated protein due to prokaryotic post-translational limitations . The absence of glycosylation does not impair its bioactivity in vitro .

In Vitro Activity

Assay SystemResults
MO7e Cell ProliferationED₅₀ = 0.3–2.6 ng/mL
NK Cell ActivationInduces CD56⁺CD16⁺KIR⁺ NK cell differentiation
T-Cell ProliferationSupports naïve CD4⁺/CD8⁺ T-cell survival and memory T-cell expansion

IL-15 Human, His activates JAK-STAT3/5, MAPK, and PI3K-AKT pathways, mirroring native IL-15 signaling . Its trans-presentation via IL-15Rα enhances receptor clustering and signaling efficiency .

Key Applications

  • Immunotherapy Development: Enhances NK and CD8⁺ T-cell populations in cancer models .

  • Inflammation Studies: Modulates immune responses in viral infections (e.g., HIV, HTLV-1) .

  • Cell Culture: Used to maintain NK/T-cell lines and primary immune cells ex vivo .

Clinical Trial Insights

Study PhaseFindings
Phase I (Subcutaneous)Safe at 2 µg/kg/day; increased circulating NK/CD8⁺ T cells in solid tumors
Phase I (Intravenous)Limited by hypotension and thrombocytopenia at higher doses

Future Directions

  • Combinatorial Therapies: Pairing with checkpoint inhibitors (e.g., anti-PD-1) to enhance tumor clearance .

  • Gene Editing: Engineering IL-15 variants with extended half-life (e.g., fused to albumin) .

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. This cytokine shares significant biological similarities with interleukin-2 (IL-2), including the ability to bind to common hematopoietin receptor subunits. As a result, they may compete for the same receptor, leading to mutual negative regulation of their activities. Maintaining a balance between this cytokine and IL-2 is essential for controlling the number of CD8+ memory cells. This cytokine initiates the activation of JAK kinases and the phosphorylation and activation of transcription factors STAT3, STAT5, and STAT6. Studies conducted on its mouse counterpart suggest that this cytokine may enhance the expression of the apoptosis inhibitor BCL2L1/BCL-x(L), potentially through the transcriptional activation function of STAT6, thereby preventing apoptosis. Two alternatively spliced transcript variants of this gene have been identified, both encoding the same protein.
Description
Recombinant Human Interleukin-15 His, produced in E. coli, is a single, non-glycosylated polypeptide chain fragment encompassing amino acids 49-162. This fragment consists of 123 amino acids with a C-terminal hexahistidine tag, resulting in a molecular weight of 13.9 kDa. The purification of IL-15 His is achieved through proprietary chromatographic techniques.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
IL-15 His is supplied in a buffer solution containing 20mM Tris-HCl (pH 8.0), 0.2mM PMSF, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For long-term storage, freeze at -20°C. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 95.0% using SDS-PAGE analysis.
Biological Activity
The biological activity is evaluated through a cell proliferation assay employing CTLL2 mouse cytotoxic T cells. The ED50 for this effect is less than 2.5 ng/ml, which corresponds to a specific activity of 400,000 units/mg.
Synonyms
IL-15, MGC9721.
Source
Escherichia Coli.
Amino Acid Sequence
MNWVNVISDL KKIEDLIQSM HIDATLYTES DVHPSCKVTA MKCFLLELQV ISLESGDASI HDTVENLIIL ANNSLSSNGN VTESGCKECE ELEEKNIKEF LQSFVHIVQM FINTSLEHHH HHH.

Product Science Overview

Introduction

Interleukin-15 (IL-15) is a cytokine that plays a crucial role in the regulation of immune responses. It is involved in the activation and proliferation of T cells and natural killer (NK) cells, which are essential components of the immune system . The recombinant form of IL-15, tagged with a histidine (His) tag, is commonly used in research to study its biological functions and potential therapeutic applications.

Gene and Protein Structure

The IL-15 gene is located on chromosome 4 and encodes a protein that consists of 162 amino acids . The recombinant form of IL-15, produced in Escherichia coli (E. coli), is a non-glycosylated polypeptide chain containing 123 amino acids (fragment 49-162) with a C-terminal hexahistidine tag . This His tag facilitates the purification of the protein using affinity chromatography techniques.

Biological Functions

IL-15 shares many biological activities with interleukin-2 (IL-2), including the ability to bind to common hematopoietin receptor subunits . It plays a significant role in the development of inflammatory and protective immune responses by modulating both innate and adaptive immune cells . IL-15 stimulates the proliferation of NK cells, T cells, and B cells, and promotes the secretion of various cytokines .

In monocytes, IL-15 induces the production of chemokines such as IL-8 and monocyte chemotactic protein 1 (CCL2), which attract neutrophils and monocytes to sites of infection . Additionally, IL-15 has been shown to increase the expression of the apoptosis inhibitor BCL2L1/BCL-x(L), potentially preventing apoptosis through the activation of transcription factors such as STAT6 .

Applications in Research

The recombinant form of IL-15 with a His tag is widely used in laboratory research to study its effects on immune cells and its potential therapeutic applications. The His tag allows for easy purification and detection of the protein, making it a valuable tool for various experimental assays .

Stability and Storage

Recombinant IL-15 (Human, His Tag) is typically supplied in a sterile filtered solution and formulated in a buffer containing Tris-HCl, PMSF, and glycerol . It should be stored at 4°C if used within 2-4 weeks, or frozen at -20°C for longer periods to maintain its stability . It is important to avoid repeated freeze-thaw cycles to preserve the protein’s activity.

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