Serial dilutions of Human IL-15 Recombinant Protein were added to CTLL-2 cells. Cell proliferation was measured and the linear portion of the curve was used to calculate the ED50.
The purity of Human IL-15 Recombinant Protein was determined by SDS-PAGE of 1 µg reduced (+) and non-reduced (-) recombinant hIL-15 and staining with Coomassie Blue.
Human IL-15 Recombinant Protein is supplied as lyophilized material that is very stable at -20°C. It is recommended to reconstitute with sterile water at a concentration of 0.1 mg/ml which can be further diluted in aqueous solutions as needed. Addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage.
A greater than or equal to 95% purity was determined by SDS-PAGE.
Endotoxin levels are less than or equal to 1 EU / 1 μg hIL-15.
The bioactivity of recombinant hIL-15 was determined in a CTLL-2 cell proliferation assay. The ED50 of each lot is less than or equal to 5 ng/ml.
Recombinant human IL-15 was expressed in E. coli and is supplied in a lyophilized form. Endotoxin levels are less than or equal to 1 EU / 1 μg hIL-15.
Interleukin-15 (IL-15) is a pleiotropic cytokine best known for inducing T cell proliferation and NK cell proliferation and activation (1,2). This glycoprotein is a member of the 4 α-helix-bundle family of cytokines and is required for the differentiation of effector CD8+ and memory phenotype CD8+ T cells (3,4). The effects of IL-5 are mediated through the heterotrimeric receptor consisting of the IL-15 receptor alpha (IL-15Rα), the β-chain, and the common γ-chain (2). The β-chain and common γ-chain are shared with the IL-2 receptor (3). Binding of IL-15 initiates signaling cascades that involve Jak1, Jak3, Stat3, and Stat5, leading to activation of the PI3K/Akt and Ras/Raf/MAPK signaling pathways (5). The effect that IL-15 has on innate and specific immunity makes it an important target for cancer immunotherapy and viral clearance (3,6).
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