Polyclonal antibody to CARD6 (CARD2)

CARDs (caspase recruitment domain) are homotypic protein-protein interaction motifs belonging to the death domain (DD) -fold superfamily (reviewed in Werts et al, 2006) . Homotypic interactions among CARD-containing proteins can occur with various proteins, including the inactive zymogen forms of caspases which have N-terminal pro-domains containing complementary CARDs. These interactions can result in the formation of multiprotein complexes, leading to protease cleavage and caspase activation. Most proteins containing a CARD are involved in signal transduction pathways that regulate apoptosis, adaptive immunity, or innate immunity including NF-kB activation and inflammation. There is a large number of CARD containing proteins, and the unique function of each remains to be fully elucidated. CARD6 is a CARD-containing protein with a domain structure that doesn't appear to be shared by any other protein (Stehlik et al, 2003) . CARD6 has been found to associate with microtubules, and is structurally and potentially functionally related to the superfamily of interferon (INF) -inducible GTPases (Dufner, 2006) . INF-inducible GTPases belong to a growing family of host defense proteins that confer cell immunity. Specifically, is thought that CARD6 may act as a pattern recognition receptor that combats pathogens in a cell-autonomous manner. CARD6 is a 1037 amino acid protein, and CINCIN1 is 311 amino acid splice variant of CARD6. This antibody recognizes both CARD6 and CINCIN1.