The binding of interleukin-1 (IL-1) to its receptor IL-1RI initiates a signaling cascade that results in the activation of NF-κB. Recently protein kinases designated IRAKs (IL-1 receptor-associated kinases) have been identified and designated as IRAK-1, IRAK-2 and IRAK-M. IRAK-2 is a serine/threonine protein kinase. The primary amino acid sequence of IRAK-2 shares similarity with that of Pelle, a protein kinase that is essential for the activation of a NF-κB homolog in Drosophila. IRAK (IL-1 receptor kinase) and mediates NF-κB activation by members of IL-1 family including IL-1 and a novel cytokine IL-18. Disruption of IRAK expression by anti-sense oligonucleotides inhibits IL-1 and IL-18-induced activation of NF-κB and activator protein, AP-1. IRAK2, an IRAK type protein kinase, is a signal transducer for the immune response interleukin-1 receptor (IL-1R) signaling cascade. IRAK2 also has been associated with signaling cell death, potentially via the Fas-associated death domain protein/caspase-8 apoptotic pathway. Dominant negative forms of IRAK2 attenuate IL-1R-mediated NF-kappa B activation, suggesting that IRAK-2 may serve as a therapeutic target for inhibiting IL-1-induced inflammation.
Immunogen
IRAK2 antibody was raised against a synthetic peptide of IRAK2 (Human).
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
IHCWB
IRAK2 antibody can be used in ELISA, Western Blot, immunohistochemistry starting at 5 μg/mL, and immunofluorescence starting at 10 μg/mL.