Interleukin 1 Receptor Associated Kinase 4 (IRAK4) Antibody
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Description
IRAK4 Antibody is a Goat Polyclonal antibody against IRAK4.
Documents del producto
Product specifications
| Category | Primary Antibodies |
| Immunogen Target | Interleukin 1 Receptor Associated Kinase 4 (IRAK4) |
| Host | Goat |
| Reactivity | Human |
| Recommended Dilution | P-ELISA: 1/32000. Optimal dilutions/concentrations should be determined by the end user. |
| Clonality | Polyclonal |
| Conjugation | Unconjugated |
| Isotype | IgG |
| Purification | Purified from goat serum by ammonium sulphate precipitation followed by antigen affinity chromatography using the immunizing peptide. |
| Size 1 | 200 µl |
| Form | Liquid |
| Tested Applications | P-ELISA, WB, IHC, IF/ICC, FCM |
| Buffer | Tris saline, pH 7.3, containing 0.02% sodium azide and 0.5% bovine serum albumin. |
| Availability | Shipped within 5-10 working days. |
| Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| Gene ID | 51135, 266632 |
| NCBI Accession | NP_057207.2, NP_001107654.1 |
| Background | Antibody anti-IRAK4 |
| Status | RUO |
| Note | Concentration: 0.5 mg/ml - |
Descripción
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IRAK4 antibody
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(PubMed:17878374). Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation to form the Myddosome together with IRAK2. Phosphorylates initially IRAK1, thus stimulating the kinase activity and intensive autophosphorylation of IRAK1. 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 NCF1 and regulates NADPH oxidase activation after LPS stimulation suggesting a similar mechanism during microbial infections.
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