Human IL-15, Tag Free (IL5-H4117) is expressed from E.coli cells. It contains AA Asn 49 - Ser 162 (Accession # P40933-1).
Predicted N-terminus: Met
This protein carries no "tag".
The protein has a calculated MW of 12.8 kDa. The protein migrates as 13 kDa under reducing (R) condition (SDS-PAGE).
Less than 0.1 EU per μg by the LAL method.
>95% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.
Contact us for customized product form or formulation.
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Human IL-15, Tag Free on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
Immobilized Human IL-15, Tag Free (Cat. No. IL5-H4117) at 2 μg/mL (100 μL/well) can bind Human IL-15 R alpha, Fc Tag (Cat. No. ILA-H5253) with a linear range of 0.6-39 ng/mL (QC tested).
Human IL-2 R beta, Fc Tag (SPR verified) (Cat. No. ILB-H5253) captured on CM5 chip via anti-human IgG Fc antibody, can bind Human IL-15, Tag Free (Cat. No. IL5-H4117) with an affinity constant of 9.5 nM as determined in a SPR assay (Biacore T200) (QC tested).
Loaded Human IL-2 R beta, Fc Tag (SPR verified) (Cat. No. ILB-H5253) on Protein A Biosensor, can bind Human IL-15, Tag Free (Cat. No. IL5-H4117) with an affinity constant of 10.2 nM as determined in BLI assay (ForteBio Octet Red96e) (Routinely tested).
活性（Bioactivity）-Cell based assay
Human IL-15, Tag Free (Cat. No. IL5-H4117) stimulates proliferation of CTLL-2 cells. The ED50 for this effect is 0.097-0.19 ng/mL (Routinely tested).
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.