Ask about this productRelated genes to: RIPK2 Blocking Peptide
- Gene:
- RIPK2 NIH gene
- Name:
- receptor interacting serine/threonine kinase 2
- Previous symbol:
- -
- Synonyms:
- RICK, RIP2, CARDIAK, CARD3
- Chromosome:
- 8q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-05-07
- Date modifiied:
- 2016-10-05
Related products to: RIPK2 Blocking Peptide
Related articles to: RIPK2 Blocking Peptide
- Receptor-interacting protein kinase 2 (RIPK2) is a multifunctional serine/threonine kinase that bridges innate immunity, inflammation, and oncogenic signaling. Downstream of NOD1 and NOD2 receptors, RIPK2 mediates NF-κB and MAPK activation through kinase-dependent and adaptor-driven mechanisms, thereby regulating cytokine production and host defense. Aberrant activation or overexpression of RIPK2 contributes to chronic inflammatory disorders and, in preclinical studies, to multiple cancers, including colorectal, breast, and lung malignancies, highlighting its dual role as a signaling integrator and potential tumor-promoting factor. Recent structural and biochemical studies have elucidated the topology of the RIPK2 kinase domain, revealing key catalytic residues (Lys47, Glu66, Asp164, Met98) and allosteric elements such as the αJ-helix and CARD domain that underpin dimerization, activation, and ubiquitination. These insights have driven the rational design of ATP-competitive, allosteric, and covalent inhibitors with improved potency and selectivity. Clinically approved multikinase inhibitors-including ponatinib, gefitinib, and regorafenib-exhibit off-target RIPK2 inhibition, while selective compounds such as WEHI-345, GSK2983559, CSLP37, UH15-15, and thienopyrimidine derivatives represent key advances in selective blockade. Novel modalities, including XIAP-BIR2 antagonists and PROTAC-based degraders, further expand therapeutic strategies for inflammation-driven diseases and, in preclinical models, cancer. Despite encouraging preclinical data, no RIPK2-specific inhibitor has yet achieved clinical approval due to safety and selectivity challenges. Continued structure-guided optimization, exploration of allosteric and degradation-based mechanisms, and integration into precision-medicine frameworks may ultimately enable safe and effective RIPK2-targeted therapies for inflammatory and autoimmune disorders, while the potential application in oncology remains under preclinical investigation. - Source: PubMed
Publication date: 2026/04/16
Al-Karmalawy Ahmed AEissa Mohamed EYousef Tarek AAl Khatib Arwa OmarHawas Samia S - To analyze the differential expression of nucleotide-binding oligomerization domain 1 (NOD1) in maternal-fetal interface cells during early and late pregnancy, and to investigate its molecular mechanisms in mediating inflammatory responses. - Source: PubMed
Deng CechuanKang HongLi NanaXue ZhiweiDeng YingWang MeixianLi LuLi YutingZhou ShuYu Ping - Receptor-interacting serine/threonine kinase 2 (RIPK2) is an important modulator of the inflammatory response in many disease states, including ischemic stroke. Here, we utilized, for the first time, a proteolysis targeting chimera (PROTAC) to specifically degrade RIPK2 in vivo in a rodent model of ischemic stroke. First, we established a dose-response curve for RIPK2 degradation following treatment with the RIPK2 PROTAC in naïve mice. Then, we assessed the time course of RIPK2 degradation and resolution to determine our optimal dosing paradigm for the acute ischemic stroke study. Interestingly, we saw significant degradation in peripheral organs but not in the brain. Using the transient middle cerebral artery occlusion (tMCAO) model of ischemic stroke, we assessed the efficacy of RIPK2 PROTAC degradation as a potential therapeutic approach for ischemic stroke. While we did not see reductions in infarct volume, we did find significant improvements in behavioral outcomes using the open field test, weight grip test, vertical grid test, and neurological deficit scoring. This study adds to the literature supporting RIPK2 as an important mediator of the post-stroke inflammatory response and further demonstrates the importance of the peripheral immune response, specifically involving the spleen, in secondary injury after ischemic stroke. - Source: PubMed
Publication date: 2026/03/15
Howell John AaronLarochelle JonathanStrawser MiaDe La Vega Mulet SolangeTishko RylandGunraj RachelLiu LeiCandelario-Jalil Eduardo - Production experience has shown that local meat duck breeds possess stronger immune capacities than commercial breeds. However, systematic comparisons of their immune differences remain insufficient, and the molecular basis underlying these differences is still unclear. - Source: PubMed
Publication date: 2026/02/27
He ZhiyuXin ShuaiChen YunyiLi XiaopengHu JiweiHe HuaLi LiangLiu HeheWang Jiwen - Pyroptosis enables host cells to eliminate intracellular pathogens effectively. However, how () evades host pyroptosis remains unclear. This study reveals that exploits the host Long non-coding RNA (lncRNA) SBF2-AS1 as a key factor to regulate the host pyroptosis. The SBF2-AS1 was significantly upregulated during infection. Knockdown of SBF2-AS1 activated NLRP3/caspase-1/GSDMD pyroptosis pathway. Mechanistically, it verified that SBF2-AS1 functions as a competing endogenous RNA for miR-196b-5p targeting RIPK2 through dual-luciferase reporter gene assay. We further identified the interaction between RIPK2 and Caspase-1 by Co-immunoprecipitation (Co-IP). Silencing SBF2-AS1 or RIPK2, as well as overexpressing miR-196b-5p, triggered pyroptosis and suppressed the replication of . In conclusion, upregulates SBF2-AS1 to increase RIPK2 by binding miR-196b-5p, which shields against pyroptosis mediated by Caspase-1 to promote its proliferation. These results uncover a novel mechanism of pathogen-host interaction and provide insights for developing new therapeutic strategies against infection. - Source: PubMed
Publication date: 2026/02/13
Wu HongrongCheng ShanYang YeweiLei WenboZhou YuLi Zhongyu