| References |
| Synonyms |
|
| Formulation |
Affinity-purified IgG |
| Stability |
1 year |
| Storage |
-20°C |
| Shipping |
Wet ice
in continental US; may vary elsewhere
|
Background Reading
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. J Biol Chem 273 12296-12300 (1998).
Kobayashi, K., Inohara, N., Hernandez, L.D., et al. RICK/Rip2/CARDIAK mediates signalling for receptors of the innate and adaptive immune systems. Nature 416 194-198 (2002).
| Size |
Global Purchasing |
| 500 µl |
|
Description
Antigen:
human RICK amino acids 11-30 (PTIPYHKLADLRYLSRGASG)
·
Host:
rabbit
·
Application(s):
WB
·
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
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. J Biol Chem 273 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 416 194-198 (2002).
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