Human IL-15 Protein (HEK293), premium grade

Interleukin 15 is also known as IL15, IL-15, and is a cytokine with structural similarity to IL-2. Like IL-2, IL-15 binds to and signals through the IL-2/IL-15 beta chain (CD122) and the common gamma chain (gamma-C, CD132) . IL-15 is secreted by mononuclear phagocytes (and some other cells) following infection by virus (es) . This cytokine induces cell proliferation of natural killer cells; cells of the innate immune system whose principal role is to kill virally infected cells. Interleukin 15 (IL-15) regulates T and natural killer (NK) cell activation and proliferation. Survival signals that maintain memory T cells in the absence of antigen are provided by IL-15. This cytokine is also implicated in NK cell development. In rodent lymphocytes, IL-15 prevents apoptosis by inducing an apoptosis inhibitor, BCL2L1/BCL-x (L) . IL-15 has been shown to enhance the anti-tumor immunity of CD8+ T cells in pre-clinical models. A phase I clinical trial to evaluate the safety, dosing, and anti-tumor efficacy of IL-15 in patients with metastatic melanoma and renal cell carcinoma (kidney cancer) has begun to enroll patients at the National Institutes of Health.

This protein carries no "tag". The protein has a calculated MW of 12.8 kDa. The protein migrates as 14-16 kDa under reducing (R) condition, and 14 kDa under non-reducing (NR) condition (SDS-PAGE) due to glycosylation.

● -20°C to -70°C for 12 months in lyophilized state; ● -70°C for 3 months under sterile conditions after reconstitution. For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Immobilized Human IL-15, premium grade (Cat. No. IL5-H5215) at 2 μg/mL (100 μL/well) can bind Human IL-2 R beta with a linear range of 1.2-39 ng/mL (Routinely tested).