Background: The mammalian homologs of the Ced-4 proteins, Apaf-1 (Ced-4), NOD1 (CARD4), and NOD2 contain a caspase recruitment domain (CARD) and a putative nucleotide binding domain, signified by a consensus Walker's A box (P-loop) and B box (Mg2+-binding site). NOD1 contains a putative regulatory domain and multiple leucine-rich repeats. NOD1 is a member of a growing family of intracellular proteins which share structural homology to the apoptosis regulator Apaf-1. NOD1 associates with the CARD-containing kinase RICK and activates NFkB. The self-association of NOD1 mediates proximity of RICK and the interaction of RICK with IKKg. In addition, NOD1 binds to multiple caspases with long prodomains, but specifically activates caspase-9 and promotes caspase-9-induced apoptosis. NOD2 is composed of two N-terminal CARDs, a nucleotide-binding domain, and multiple C-terminal leucine-rich repeats. The expression of NOD2 is highly restricted to monocytes, and activates NFkB in response to bacterial lipopoly-saccharides.
Description: Rabbit polyclonal to CARD15
Immunogen: KLH conjugated synthetic peptide derived from CARD15
Specificity: ·Reacts with Human, Mouse and Rat.
·Isotype: IgG
Application: ·Western blotting: 1/100-500. Predicted Mol wt: 115 kDa;
·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;
·Immunocytochemistry/Immunofluorescence: 1/100;
·Immunoprecipitation: 1/50;
·ELISA: 1/500;
·Optimal working dilutions must be determined by the end user.
