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>   首页   >   产品   >   一抗   >   精选抗体   >   磷酸化抗体   >   Phospho-IRAK1(S376) Antibody   

Phospho-IRAK1(S376) Antibody

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - Phospho-IRAK1(S376) Antibody AP50215
    Western blot analysis of extracts from MCF-7 cells,untreated or treated with Calyculin A,using Phospho-IRAK1(S376) Antibody.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, IHC-P, IHC-F, IF, ICC, E
Primary Accession P51617
Reactivity Mouse, Rat, Drosophila
Host Rabbit
Clonality Polyclonal
Calculated MW 76537 Da
Physical State Liquid
Immunogen KLH conjugated Synthesised phosphopeptide derived from human IRAK1 around the phosphorylation site of Ser376
Epitope Specificity QS(p-S)TV
Isotype IgG
Purity affinity purified by Protein A
Buffer 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
SUBCELLULAR LOCATION Cytoplasm. Nucleus. Note=Translocates to the nucleus when sumoylated.
SIMILARITY Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. Pelle subfamily. Contains 1 death domain. Contains 1 protein kinase domain.
SUBUNIT Homodimer. Interacts with TOLLIP; this interaction occurs in the cytosol prior to receptor activation. Interacts with MYD88; this interaction recruits IRAK1 to the stimulated receptor complex. Interacts with IL1RL1. Interacts with IRAK1BP1. Associates with TRAF6, PELI1 and IRAK4; this complex recruits MAP3K7/TAK1, TAB1 and TAB2 to mediate NF-kappa-B activation. Interacts (when polyubiquitinated) with IKBKG/NEMO.
Post-translational modifications Following recruitment on the activated receptor complex, phosphorylated on Thr-209, probably by IRAK4, resulting in a conformational change of the kinase domain, allowing further phosphorylations to take place. Thr-387 phosphorylation in the activation loop is required to achieve full enzymatic activity. Polyubiquitinated after cell stimulation with IL-1-beta by PELI1, PELI2 and PELI3. Polyubiquitination occurs with polyubiquitin chains linked through 'Lys-63'. Ubiquitination promotes interaction with NEMO/IKBKG. Also sumoylated; leading to nuclear translocation.
Important Note This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
Background Descriptions This gene encodes the interleukin-1 receptor-associated kinase 1, one of two putative serine/threonine kinases that become associated with the interleukin-1 receptor (IL1R) upon stimulation. This gene is partially responsible for IL1-induced upregulation of the transcription factor NF-kappa B. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]
Additional Information
Gene ID 3654
Other Names Interleukin-1 receptor-associated kinase 1, IRAK-1, IRAK1, IRAK
Target/Specificity Isoform 1 and isoform 2 are ubiquitously expressed in all tissues examined, with isoform 1 being more strongly expressed than isoform 2.
Dilution WB=1:500-2000,IHC-P=1:100-500,IHC-F=1:100-500,ICC=1:100,IF=1:100-500,Flow-Cyt=1ug/test,ELISA=1:5000-10000
Format0.01M TBS(pH7.4) with 1% BSA, 0.09% (W/V) sodium azide and 50% Glyce
StorageStore at -20 °C for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.
Protein Information
Name IRAK1 (HGNC:6112)
Synonyms IRAK
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.
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

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.

REFERENCES

Cao Z.,et al.Science 271:1128-1131(1996).
Reichwald K.,et al.Mamm. Genome 11:182-190(2000).
Jensen L.E.,et al.J. Biol. Chem. 276:29037-29044(2001).
Rao N.,et al.Mol. Cell. Biol. 25:6521-6532(2005).
Ross M.T.,et al.Nature 434:325-337(2005).

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