The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/50 - 1/100.
FunctionBinds to the IL-1 type I receptor following IL-1 engagement, triggering intracellular signaling cascades leading to transcriptional up-regulation and mRNA stabilization. Isoform 1 binds rapidly but is then degraded allowing isoform 2 to mediate a slower, more sustained response to the cytokine. Isoform 2 is inactive suggesting that the kinase activity of this enzyme is not required for IL-1 signaling. Once phosphorylated, IRAK1 recruits the adapter protein PELI1.
Tissue specificityIsoform 1 and isoform 2 are ubiquitously expressed in all tissues examined, with isoform 1 being more strongly expressed than isoform 2.
Sequence similaritiesBelongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. Pelle subfamily. Contains 1 protein kinase domain.
Post-translational modificationsAutophosphorylated or is transphosphorylated by IRAK4 following recruitment to the IL-1RI. In the case of isoform 1, this is linked to ubiquitination and degradation. Polyubiquitinated; after cell stimulation with IL-1-beta. Polyubiquitination occurs with polyubiquitin chains linked through 'Lys-63'.
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - IRAK antibody (ab62700)
ab62700, at 1/50 dilution, staining IRAK in paraffin embedded human breast carcinoma tissue by Immunohistochemistry in the absence or presence of the immunising peptide.
References for Anti-IRAK antibody (ab62700)
This product has been referenced in:
Ahmad R et al. Increased expression of the interleukin-1 receptor-associated kinase (IRAK)-1 is associated with adipose tissue inflammatory state in obesity. Diabetol Metab Syndr7:71 (2015).
Read more (PubMed: 26312071) »