RICK Polyclonal Antibody

Apoptosis is mediated by death domain (DD) and/or caspase recruitment domain (CARD) containing molecules and a caspase family of proteases. The DD-containing serine/threonine kinase RIP regulates Fas-induced apoptosis. A novel CARD-containing serine/threonine kinase that regulates apoptosis was identified and designated RICK for RIP-like interacting CLARP kinase.¹ RICK contains an N-terminal kinase catalytic domain and a C-terminal CARD domain. The RICK kinase domain has high sequence homology to that of RIP. Overexpression of RICK promotes the activation of caspase-8 and Fas-induced apoptosis. RICK represents a novel kinase that regulates Fas-induced apoptosis. The mRNA for RICK is expressed in multiple human tissues.¹ RICK interacts with several Nod and T-cell receptor proteins and thereby confers signal transduction for innate and adaptive immune system responses.²

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1. Inohara, N., del Peso, L., Koseki, T., et al. RICK, a novel protein kinase containing a caspase recruitment domain, interacts with CLARP and regulates CD95-mediated apoptosis. The Journal of Biological Chemisty 273(29), 12296-12300 (1998).

2. Kobayashi, K., Inohara, N., Hernandez, L.D., et al. RICK/Rip2/CARDIAK mediates signalling for receptors of the innate and adaptive immune systems. Nature 416(6877), 194-198 (2002).