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.