Rabbit Polyclonal
ELISA | 1:2000 |
WB | 1:1000 |
Size 100 μl
Species Reactivity Hu, Rt, Ms
MW 110 kDa
The nucleotide-binding oligomerization domain (NOD)-like receptor (NLR) family is a diverse family of cytoplasmic innate immune receptors that are involved in recognition of pathogen-associated molecular patterns. NLRs are important for pathogen sensing, transcriptional activation of proinflammatory cytokines and activation of inflammatory caspases. NLRC4 (IPAF, CARD12) forms the inflammasome that responds to bacterial flagellin. This inflammasome is activated by NLRC4 oligomerization, NAIP protein binding, and activation of caspase-1 leading to pyroptosis. NLRC4 is phosphorylated on Ser-533 by PKCδ following infection of macrophages with S. typhimurium. Mutant forms of NLRC4 demonstrate that an unphosphorylatable form (S533A) does not activate caspase-1 and pyroptosis in response to S. typhimurium, while a phosphomimetic NLRC4 (S533D) mutant causes rapid macrophage pyroptosis without infection. Thus, PKCδ phosphorylation of NLRC4 (S533) may be a critical event in inflammasome activation and host innate immunity.
References
Elinav, E. et al. (2011) Immunity 34:665.
Poyet, J.L. et al. (2001) J Biol Chem 276:28309.
Western blot image of mouse recombinant NLRC4 (Ser-533) phosphorylated peptide (lanes 1 & 4) and dephosphorylated peptide (lanes 2 & 5), as well as human PMA-differentiated THP1 cells (lanes 3 & 6). The blots were probed with rabbit polyclonals anti-NLRC4 (a.a. 525-538) (lanes 1-3) and anti-NLRC4 (Ser-533) phospho-specific (lanes 4-6).
*For more information, see UniProt Accession Q3UP24
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
This kit contains: