Recombinant Human IRAK1

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Product specifications
Category | Proteins and Peptides |
Host | E.Coli |
Reactivity | Human |
Assay Data | Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg/ml by gently pipetting 2-3 times, don't vortex. |
Recommended Dilution | ¥ |
Isotype | ¥ |
Clone ID | ¥ |
Observed MW | 50 kDa |
Expression | 504-712 |
Purity | Greater than 90% as determined by SDS-PAGE. |
Size 1 | 50μg |
Size 2 | 200μg |
Size 3 | 1mg |
Form | Lyophilized powder |
Tested Applications | Western Blot, ELISA |
Buffer | Lyophilized from a 0.2 μm filtered solution in 10 mM Hepes, 500 mM NaCl with 5% trehalose, pH 7.4. |
Availability | 7 days |
Storage | The lyophilized protein is stable at -20 °C for up to 1 year. After reconstitution, the protein solution is stable at -20 to -80 °C for 3 months or 1 week at 2 to 8 °C under sterile conditions. For extended storage, it is recommended to further dilute in working aliquots, avoid repeated freeze/thaw cycle. |
UniProt ID | P51617 |
Alias | EC 2.7.11, EC 2.7.11.1, Il1rak, interleukin-1 receptor-associated kinase 1, IRAK1, IRAK-1, IRAKPelle homolog, Pelle, Plpk |
Background | Protein IRAK1 |
Status | RUO |
Note | Tag : N-terminal GST tag |
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IRAK1 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. 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.
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IRAK1 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. 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.
Ver Producto