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Validated All-in-One™ qPCR Primer for RIPK2(NM_003821.5) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
This gene encodes a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases. The encoded protein contains a C-terminal caspase activation and recruitment domain (CARD), and is a component of signaling complexes in both the innate and adaptive immune pathways. It is a potent activator of NF-kappaB and inducer of apoptosis in response to various stimuli. [provided by RefSeq].
Gene References into function
- Involvement of receptor-interacting protein 2 in innate and adaptive immune responses
- Rip2 transduces signals from both innate and adaptive immune responses. Functions downstream of the TLR2/3/4, IL-1 and IL-18 receptors.
- These results implicate RIP2 in a previously unrecognized role: a checkpoint for myogenic proliferation and differentiation.
- equilibrium and kinetic folding of a unique protein domain, caspase recruitment domain (CARD), of the RIP-like interacting CLARP kinase (RICK) (RICK-CARD), which adopts a alpha-helical Greek key fold
- role in CARD6 modulation of NF-kappa B activation
- Rip2 has an important role in TCR-induced NF-kappaB activation and T-cell function
- NOD2-dependent ubiquitinylation of NEMO (a key component of the NF-kB signaling complex) is dependent on the scaffolding protein kinase RIP2.
- Caspase-1-mediated cell death is regulated, at least in part, by the balance of Rip2 and Cop; alterations of this balance may contribute to aberrant caspase-1-mediated pathogenesis in Huntington's disease.
- CARD6 is a regulator of NF-kappaB activation that modulates the functions of RICK protein
- NOD2-S interacts with both, NOD2 and receptor-interacting protein kinase 2 and inhibits the "nodosome" assembly by interfering with the oligomerization of NOD2
- review of the regulation of interactions of CARD6 with RICK and microtubules [review]
- Results indicate that S176 is a regulatory autophosphorylation site for RIP2 and that S176 phosphorylation can be used to monitor the activation state of RIP2.
- Cop inhibition of cell death, at least to a certain extent, results from its interference with the activation of caspase-1 and caspase-4.
- mutational analysis shows that interaction of NOD1 with RICK is critically dependent on 3 acidic residues on NOD1 CARD & 3 basic residues on RICK CARD & is likely to have a strong electrostatic component
- Although polymorphisms in RIP2 are not likely to be associated with the development of asthma, the genetic variants might contribute to asthma severity in the Japanese population
- NOD2 is responsible for the membrane recruitment of RICK to induce a regulated NF-kappaB signaling and production of proinflammatory cytokines.
- RIPK2 is a marker for resolution of peritoneal dialysis-associated peritonitis.
- Data show that RICK polyubiquitination links TAK1 to IKK complexes, a critical step in Nod1/Nod2-mediated NF-kappaB activation.
- The encapsulation efficiency of RIPK2 is reported.
- We conclude that the endogenous IL-8 response induced by C. trachomatis infection is dependent upon NOD1 signaling through RIP2 as part of a signal system requiring multiple inputs for optimal IL-8 induction.
- upregulation of RIP2 expression is required for rapid resolution of peritonitis
