|Application ||WB, IF, ICC, E|
|Other Accession||O43353, 8767|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||Predicted: 59 kDa |
Observed: 60 kDa
|Application Notes||RICK antibody can be used for detection of RICK by Western blot at 1 μg/mL. Antibody can also be used for immunocytochemistry starting at 10 μg/mL. For immunofluorescence start at 20 μg/mL.|
|Other Names||RICK Antibody: CCK, RICK, RIP2, CARD3, GIG30, CARDIAK, UNQ277/PRO314/PRO34092, CARD-containing interleukin-1 beta-converting enzyme-associated kinase, CARD-containing IL-1 beta ICE-kinase, receptor-interacting serine-threonine kinase 2|
|Target/Specificity||RICK antibody was raised against a peptide corresponding to 20 amino acids near the amino terminus of human RICK.|
The immunogen is located within the first 50 amino acids of RICK.
|Reconstitution & Storage||RICK antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||RICK Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||CARDIAK, RICK, RIP2|
|Function||Serine/threonine/tyrosine kinase that plays an essential role in modulation of innate and adaptive immune responses. Upon stimulation by bacterial peptidoglycans, NOD1 and NOD2 are activated, oligomerize and recruit RIPK2 through CARD-CARD domains. Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3. The polyubiquitinated protein mediates the recruitment of MAP3K7/TAK1 to IKBKG/NEMO and induces 'Lys-63'-linked polyubiquitination of IKBKG/NEMO and subsequent activation of IKBKB/IKKB. In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Plays also a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation.|
|Tissue Location||Detected in heart, brain, placenta, lung, peripheral blood leukocytes, spleen, kidney, testis, prostate, pancreas and lymph node|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
email@example.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
RICK Antibody: Apoptosis is mediated by death domain (DD) and/or caspase recruitment domain (CARD) containing molecules and a caspase family of proteases. DD-containing serine/threonine kinase RIP regulates Fas-induced apoptosis. A novel CARD-containing serine/threonine kinase was recently identified and designated RICK/RIP2/CARDIAK for RIP-like interacting CLARP kinase, receptor interacting protein-2, and CARD-containing ICE associated kinase, respectively. RICK contains an N-terminal kinase catalytic domain and a C-terminal CARD domain. Overexpression of RICK induced apoptosis and activation of NF-κB and JNK. RICK interacts with members of the TRAF family, CLARP and caspase-1. Thus, RICK represents a novel kinase that regulates TNF and Fas induced-apoptosis and that is involved in the generation of proinflammatory cytokine IL-1β. The messenger RNA of RICK is expressed in multiple human tissues.
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. 1998; 273:12296-300.
McCarthy JV, Ni J, and Dixit VM. RIP2 is a novel NF-κB-activating and cell death-inducing kinase. J. Biol. Chem. 1998; 273:16968-75.
Thome M, Hofmann K, Burns K, et al. Identification of CARDIAK, a RIP-like kinase that associates with caspase-1. Curr. Biol. 1998; 8:885-8.
If you have used an Abgent product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at firstname.lastname@example.org.