IL-1α (human) (rec.)
|Synonyms||Interleukin-1α; IL-1F1; IL-1A|
|Source/Host||HEK 293 cells|
|Sequence||Human IL-1α (aa 113-271).|
|Biological Activity||The ED50 as determined by the dose-dependent stimulation of murine D10S cells is ≤ 0.001 ng/ml, corresponding to a specific activity of ≥ 1 x 109units/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_000566.3: IL-1α (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|
The most prominent members of the interleukin-1 (IL-1) superfamily are IL-1α and IL-1β. They lack a signal peptide and are secreted by an unconventional, endoplasmic reticulum-Golgi-independent mechanism. IL-1α was reported to be more widely and constitutively expressed and has intracellular functions, but also acts locally in a membrane-bound form by activating IL-1R1. Additionally, passive release of IL-1α upon cell death can trigger a sterile inflammatory response to dying cells. The cleavage of IL-1α is not mediated by caspase-1 and is not required for binding to IL-1R1. Recently it has been observed that all activators of the inflammasome NLRP3/NALP3 induce the simultaneous secretion of IL-1α and IL-1β. Although most activators fully rely on the inflammasome for IL-1α secretion, some induce the processing and secretion of IL-1α in an inflammasome-independent manner.