IL-1alpha (human) (rec.) (His)

Interleukin-1alpha; IL-1F1; IL-1A

32160000

<1EU/µg protein (LAL test; Lonza).

liquid

Lyophilized from a concentrated sterile solution containing 50mM Tris-HCl buffer (pH 8.0) and 100mM NaCl.

Avoid freeze/thaw cycles.Centrifuge lyophilized vial before opening and reconstitution.

Protein. Human IL-1alpha (aa 113-271) is fused at the C-terminus to a His-tag. Source: E. coli. Endotoxin content: <0.1EU/µg protein (LAL test; Lonza). Lyophilized from a concentrated sterile solution containing 50mM Tris-HCl buffer (pH 8.0) and 100mM NaCl. Purity: >98% (SDS-PAGE). 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.

NP_000566.3

Plastic Vial

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.

>95% (SDS-PAGE)

Human IL-1alpha (aa 113-271) is fused at the C-terminus to a His-tag.

E. coli

His

Non-hazardous

Interleukins

41116127

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.