|Application ||WB, IHC-P, E|
|Calculated MW||76537 Da|
|Antigen Region||683-712 aa|
|Other Names||Interleukin-1 receptor-associated kinase 1, IRAK-1, IRAK1, IRAK|
|Target/Specificity||This IRAK antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 683-712 amino acids from the C-terminal region of human IRAK.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||IRAK Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor- signaling complex upon TLR activation. Association with MYD88 leads to IRAK1 phosphorylation by IRAK4 and subsequent autophosphorylation and kinase activation. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates the interferon regulatory factor 7 (IRF7) to induce its activation and translocation to the nucleus, resulting in transcriptional activation of type I IFN genes, which drive the cell in an antiviral state. When sumoylated, translocates to the nucleus and phosphorylates STAT3.|
|Cellular Location||Cytoplasm. Nucleus. Lipid droplet. Note=Translocates to the nucleus when sumoylated RSAD2/viperin recruits it to the lipid droplet (By similarity)|
|Tissue Location||Isoform 1 and isoform 2 are ubiquitously expressed in all tissues examined, with isoform 1 being more strongly expressed than isoform 2.|
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Provided below are standard protocols that you may find useful for product applications.
Protein kinases are enzymes that transfer a phosphate group from a phosphate donor, generally the g phosphate of ATP, onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. With more than 500 gene products, the protein kinase family is one of the largest families of proteins in eukaryotes. The family has been classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. The tyrosine-like kinase (TLK) group consists of 40 tyrosine and serine-threonine kinases such as MLK (mixed-lineage kinase), LISK (LIMK/TESK), IRAK (interleukin-1 receptor-associated kinase), Raf, RIPK (receptor-interacting protein kinase), and STRK (activin and TGF-beta receptors) families.
Jensen, L.E., et al., J. Immunol. 171(3):1500-1506 (2003).
Jiang, Z., et al., J. Biol. Chem. 278(13):10952-10956 (2003).
Cao, Z., et al., Science 271(5252):1128-1131 (1996).
Strelow, A., et al., FEBS Lett. 547 (1-3), 157-161 (2003).
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