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.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of NOD1 of mouse, rat and human origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 715-890 mapping near the C-terminus of NOD1 of human origin
Tissue Specificity
epitope corresponding to amino acids 715-890 mapping near the C-terminus of NOD1 of human origin