About this item
The most prominent members of the interleukin-1 (IL-1) superfamily are IL-1alpha and IL-1beta. They lack a signal peptide and are secreted by an unconventional, endoplasmic reticulum-Golgi-independent mechanism. IL-1alpha 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-1alpha upon cell death can trigger a sterile inflammatory response to dying cells. The cleavage of IL-1alpha 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-1alpha and IL-1beta. Although most activators fully rely on the inflammasome for IL-1alpha secretion, some induce the processing and secretion of IL-1alpha in an inflammasome-independent manner.
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Specifications
- Conjugation:Unconjugated
- Protein Function:Interleukins
- Protein/Peptide Type:Recombinant
- Source:E. coli
- Species:Human
- Storage Conditions:–20 °C
- Endotoxin Content:<0.1EU/µg
- Gene ID:NP_000566.3
- Protein Synonyms:IL-1F1|Interleukin-1alpha|IL-1A
- Protein/Peptide Name:IL-1alpha
- Purity:98%
- Endotoxin Level:Low
- Formulation:Lyophilized from a concentrated sterile solution containing 50mM Tris-HCl buffer (pH 8.0) and 100mM NaCl.
- Shipping Temperature:-20 °C, Blue Ice