RICK Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IF, ICC, E |
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Primary Accession | O43353 |
Other Accession | O43353, 8767 |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | IgG |
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. |
Gene ID | 8767 |
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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. |
Name | RIPK2 {ECO:0000303|PubMed:30026309, ECO:0000312|HGNC:HGNC:10020} |
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Function | Serine/threonine/tyrosine-protein kinase that plays an essential role in modulation of innate and adaptive immune responses (PubMed:14638696, PubMed:17054981, PubMed:21123652, PubMed:28656966, PubMed:9575181, PubMed:9642260). Acts as a key effector of NOD1 and NOD2 signaling pathways: upon activation by bacterial peptidoglycans, NOD1 and NOD2 oligomerize and recruit RIPK2 via CARD-CARD domains, leading to the formation of RIPK2 filaments (PubMed:17054981, PubMed:17562858, PubMed:21123652, PubMed:22607974, PubMed:28656966, PubMed:29452636, PubMed:30026309). Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3, as well as 'Met-1'-linked (linear) polyubiquitination by the LUBAC complex, becoming a scaffolding protein for downstream effectors (PubMed:22607974, PubMed:28545134, PubMed:29452636, PubMed:30026309, PubMed:30279485, PubMed:30478312). 'Met-1'-linked polyubiquitin chains attached to RIPK2 recruit IKBKG/NEMO, which undergoes 'Lys-63'-linked polyubiquitination in a RIPK2-dependent process (PubMed:17562858, PubMed:22607974, PubMed:29452636, PubMed:30026309). 'Lys-63'-linked polyubiquitin chains attached to RIPK2 serve as docking sites for TAB2 and TAB3 and mediate the recruitment of MAP3K7/TAK1 to IKBKG/NEMO, inducing subsequent activation of IKBKB/IKKB (PubMed:18079694). 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 (PubMed:18079694). The protein kinase activity is dispensable for the NOD1 and NOD2 signaling pathways (PubMed:29452636, PubMed:30026309). Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappa-B activation by NOD2 (PubMed:21887730). Also involved in adaptive immunity: plays a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation (PubMed:14638696). Plays a role in the inactivation of RHOA in response to NGFR signaling (PubMed:26646181). |
Cellular Location | Cytoplasm. Cell membrane; Peripheral membrane protein. Endoplasmic reticulum. Note=Recruited to the cell membrane by NOD2 following stimulation by bacterial peptidoglycans |
Tissue Location | Detected in heart, brain, placenta, lung, peripheral blood leukocytes, spleen, kidney, testis, prostate, pancreas and lymph node. |
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Background
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.
References
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.
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