Rabbit Polyclonal Phospho-IRAK1(S376) Antibody

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     Western blot analysis of lysates from Hela cell line, untreated or treated with IL-1 beta(20ng/ml) + Calyculin A(100nM), using (Cat.  #P34444)(upper) or Tubulin (lower).    

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     Immunofluorescent analysis of 4% paraformaldehyde-fixed, 0.1% Triton X-100 permeabilized HeLa (human cervical epithelial adenocarcinoma cell line) cells labeling IRAK1 with P34444 at 1/25 dilution, followed by Dylight® 488-conjugated goat anti-rabbit IgG  secondary antibody at 1/200 dilution (green). Immunofluorescence image showing cytoplasm and nuclear speckles staining on HeLa cell line. Cytoplasmic actin is detected with Dylight® 554 Phalloidin  at 1/100 dilution (red). The nuclear counter stain is DAPI (blue).    

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     P34444 staining IRAK1 in human kidney tissue sections by Immunohistochemistry (IHC-P - paraformaldehyde-fixed,  paraffin-embedded sections).  Tissue was fixed with formaldehyde and blocked with 3% BSA for 0. 5 hour at room temperature; antigen retrieval was by heat mediation with a citrate buffer (pH6).  Samples were incubated with primary antibody (1/25) for 1 hours at 37°C.  A undiluted biotinylated goat polyvalent antibody was used as the secondary antibody.    

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     P34444 staining IRAK1 in human testis tissue sections by Immunohistochemistry (IHC-P - paraformaldehyde-fixed,  paraffin-embedded sections).  Tissue was fixed with formaldehyde and blocked with 3% BSA for 0. 5 hour at room temperature; antigen retrieval was by heat mediation with a citrate buffer (pH6).  Samples were incubated with primary antibody (1/25) for 1 hours at 37°C.  A undiluted biotinylated goat polyvalent antibody was used as the secondary antibody.    

The Phospho-IRAK1(S376) antibody detects the phosphorylated form of interleukin-1 receptor-associated kinase 1 (IRAK1) at serine residue 376. IRAK1 is a critical serine/threonine kinase in innate immune signaling, primarily activated downstream of Toll-like receptors (TLRs) and the interleukin-1 receptor (IL-1R) family. Upon receptor activation, IRAK1 is recruited to receptor complexes via adaptor proteins like MyD88. leading to its phosphorylation and subsequent activation. Phosphorylation at specific residues, including S376. regulates IRAK1’s kinase activity, interaction with signaling partners (e.g., TRAF6), and downstream activation of NF-κB and MAPK pathways, which drive pro-inflammatory cytokine production.

The Phospho-IRAK1(S376) antibody is widely used to study IRAK1 activation dynamics in immune responses, inflammatory diseases (e.g., sepsis, rheumatoid arthritis), and cancer. Researchers employ it in techniques such as Western blotting, immunofluorescence, and immunoprecipitation to assess IRAK1 phosphorylation status under conditions like pathogen exposure, cytokine stimulation, or therapeutic intervention. Specificity validation via phosphatase treatment or kinase-deficient mutants is essential to confirm target recognition. This antibody also aids in evaluating IRAK1-targeted therapies, as aberrant IRAK1 signaling is linked to autoimmune disorders and tumor progression. Understanding IRAK1 phosphorylation at S376 provides insights into immune regulation and potential therapeutic strategies.