Serial dilutions of Mouse IL-2 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 Mouse IL-2 Recombinant Protein was determined by SDS-PAGE of 1 µg reduced (+) and non-reduced (-) recombinant mIL-2 and staining with Coomassie Blue.
Mouse IL-2 Recombinant Protein is supplied as lyophilized material that is very stable at -20°C. It is recommended to reconstitute with sterile 10 mM acetic acid 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 mIL-2.
The bioactivity of recombinant mIL-2 was determined in a CTLL-2 cell proliferation assay. The ED50 of each lot is less than or equal to 5 ng/ml.
Recombinant mouse IL-2 was expressed in E. coli and is supplied in a lyophilized form.
Interleukin-2 (IL-2) is a T cell stimulatory cytokine best known for inducing T cell proliferation and NK cell proliferation and activation (1,2). IL-2 also promotes peripheral development of regulatory T cells (Tregs) (3,4). Conversely, IL-2 is involved in the activation-induced cell death (AICD) that is observed post T cell expansion by increasing levels of Fas on CD4+ T cells (5). The effects of IL-2 are mediated through a trimeric receptor complex consisting of IL-2Rα, IL-2Rβ, and the common gamma chain, γc (1,2). IL-2Rα binds exclusively to IL-2 with low affinity and increases the binding affinity of the whole receptor complex including IL-2Rβ and γc subunits. IL-15 also binds to IL-2Rβ (1,2). γc is used by other cytokines including IL-4, IL-7, IL-9, IL-15, and IL-21 (1,2). Binding of IL-2 initiates signaling cascades involving Jak1, Jak3, Stat5, and the PI3K/Akt pathways (1,2).
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