More Information Product Details
Synonyms Interleukin-2; Aldesleukin |
Product Type Protein |
Properties
Source/Host HEK 293 cells |
Sequence Human IL-2 (aa 21-153) (mutation C145S) is fused at the C-terminus to a His-tag. |
Crossreactivity HumanMouse |
Biological Activity Measured by its ability to stimulate the proliferation of mouse CTLL-2 cells. The ED50 for this effect is typically 0.1ng/mL, corresponding to a specific activity of 1x 107 units/mg. |
MW ~19kDa (SDS-PAGE) |
Purity ≥95% (SDS-PAGE) |
Endotoxin Content |
Reconstitution Reconstitute 10µg vial with 100 µl sterile water to a concentration of 0.1mg/ml. Reconstitute 50µg vial with 100 µl sterile water to a concentration of 0.5mg/ml. Add 1X PBS to the desired protein concentration. |
Formulation Lyophilized from 0.2μm-filtered solution in PBS. |
Other Product Data NCBI reference NP_000577.2: IL-2 (human) |
Declaration Manufactured by Chimerigen. |
Shipping and Handling
Shipping BLUE ICE |
Short Term Storage +4°C |
Long Term Storage -20°C |
Handling Advice Avoid freeze/thaw cycles.PBS containing at least 0.1% BSA should be used for further dilutions. |
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.Working aliquots are stable for up to 3 months when stored at -20°C. |
Documents
MSDS No |
Product Specification Sheet
Datasheet Download PDF |
Interleukin-2 (IL-2) is a 133 amino acid glycoprotein with one intramolecular disulfide bond and variable glycosylation. It is secreted by activated T cells and induces proliferation and maturation of activated T cells, natural killer cells, and lymphokine activated killer cells. IL-2 also stimulates proliferation of antibody-producing B cells, activates neutrophils, and induces mononuclear cells to secrete IFN-γ and TNF-α and -β. Moreover, studies have shown that IL-2 is required for activation-induced apoptosis, an important hemeostatic mechanism in the immune system, which is involved in the maintenance of peripheral tolerance to self-antigens. The modified IL-2 protein containing a substitution at position C145S retains full biological activity, suggesting that the cysteine at this position is not involved in a disulfide bond and that a free sulfhydryl group at that position is not necessary for receptor binding. Additionally, the C145S mutation insertion avoids non-specific disulfides and improves the physical properties of the protein.