IL-2 (C145S Mutant) (human) (rec.) (His)
225 CHF CHF 225.00
CHI-HF-20102-C01010 µgCHF 225.00
CHI-HF-20102-C05050 µgCHF 675.00
|Source/Host||HEK 293 cells|
|Sequence||Human IL-2 (aa 21-153) (mutation C145S) is fused at the C-terminus to a His-tag.|
|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.|
|Endotoxin Content||<0.01EU/μg protein (LAL test; Lonza).|
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|
|Short Term Storage||+4°C|
|Long Term Storage||-20°C|
Avoid freeze/thaw cycles.
PBS containing at least 0.1% BSA should be used for further dilutions.
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.
|Product Specification Sheet|
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.