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

Research Use Only
CHI-HR-20001A
Chimerigen Laboratories
Product group Proteins / Signaling Molecules
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Overview

  • Supplier
    Chimerigen Laboratories
  • Product Name
    IL-1alpha (human) (rec.) (His)
  • Delivery Days Customer
    10
  • Certification
    Research Use Only
  • Estimated Purity
    >95%
  • Scientific Description
    Protein. Human IL-1alpha (aa 113-271) is fused at the C-terminus to a His-tag. Source: E. coli. Endotoxin content: <0.1EU/microg 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. - 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.
  • Storage Instruction
    -20°C,2°C to 8°C
  • UNSPSC
    12352202