As seen on the dot blots (Figures 1-2), these antibodies are specific for the phosphothreonine sequence and not the non-phosphothreonine sequence. As well, the cross-reactivity between the pThr209 and pThr 387 antibodies is minimal (Figure 3).
Interleukin-1 (IL-1) receptor-associated kinase (IRAK) is a serine/threonine-specific kinase (1). The mammalian family of IRAK molecules contains four members (IRAK1, IRAK2, IRAK3/IRAK-M and IRAK4). The binding of IL-1 to IL-1 receptor type I (IL-1RI) initiates the formation of a complex that includes IL-1RI, AcP, MyD88 and IRAKs (2). IRAK undergoes autophosphorylation shortly after IL-1 stimulation and serves as a signaling molecule to mediate IL-1 response (3). IRAK mediates a signaling cascade leading to NF-KB activation by members in IL-1 family including IL-1 and a novel cytokine IL-18 (also termed IGIF) (1, 4).
Rabbit anti-IRAK-1(pThr209) – cat# 55331 polyclonal antibody was raised against a peptide corresponding to human IRAK1 at the phosphorylated threonine 209 (EISRGpTH), while Rabbit anti-IRAK-1(pThr387) – cat# 55333 polyclonal antibody corresponds to human IRAK1 at the phosphorylated threonine 387 (VRG-pTLAY). The non-phosphorylated version of these antibodies is also available. The IRAK1 antibodies have been evaluated for specificity by dot blot.
1. Dinarello, CA. Blood 87, 2095-2147 (1996).
2. Takaesu, G. et al. Mol. Cell. Biol. 21, 2475-2484 (2001).
3. Jianing H. et al. Proc. Natl. Acad. Sci. USA 94, 12829 (1997).
4. Robinson D. et al. Immunity 7, 571 (1997).
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