IL-1α (human) (rec.) (His)
|Synonyms||Interleukin-1α; IL-1F1; IL-1A|
Human IL-1α (aa 113-271) is fused at the C-terminus to a His-tag.
|Endotoxin Content||<1EU/μg protein (LAL test; Lonza).|
|Reconstitution||Reconstituted in sterile H2O not less than 100μg/ml, which can then be further diluted in other aqueous solutions.|
|Formulation||Lyophilized from a concentrated sterile solution containing 50mM Tris-HCl buffer (pH 8.0) and 100mM NaCl.|
|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|
|Handling Advice||Avoid freeze/thaw cycles.|
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.