{"product_id":"cst-88918v2","title":"CST,  88918V2, PathScan® RP Phospho-RIP (Ser166) Chemiluminescent Sandwich ELISA Kit","description":"ELISA Kit for studying RIPK1 (Ser166) phosphate in the research area.\n\n\u003cb\u003eProtocol\u003c\/b\u003e\nAvailable protocols: ELISA+\n\u003cb\u003eSpecificity \/ Sensitivity\u003c\/b\u003e\nThe PathScan\nSpecies Reactivity: Human, Mouse\n\u003cb\u003eBackground\u003c\/b\u003e\nThe receptor-interacting protein (RIP) family of serine-threonine kinases (RIP, RIP2, RIP3, and RIP4) are important regulators of cellular stress that trigger pro-survival and inflammatory responses through the activation of NF-κB, as well as pro-apoptotic pathways (1). In addition to the kinase domain, RIP contains a death domain responsible for interaction with the death domain receptor Fas and recruitment to TNF-R1 through interaction with TRADD (2,3). RIP-deficient cells show a failure in TNF-mediated NF-κB activation, making the cells more sensitive to apoptosis (4,5). RIP also interacts with TNF-receptor-associated factors (TRAFs) and can recruit IKKs to the TNF-R1 signaling complex via interaction with NEMO, leading to IκB phosphorylation and degradation (6,7). Overexpression of RIP induces both NF-κB activation and apoptosis (2,3). Caspase-8-dependent cleavage of the RIP death domain can trigger the apoptotic activity of RIP (8). Necroptosis, a regulated pathway for necrotic cell death, is triggered by a number of inflammatory signals including cytokines in the tumor necrosis factor (TNF) family, pathogen sensors such as toll-like receptors (TLRs), and ischemic injury (9,10). The process is negatively regulated by caspases and is initiated through a complex containing the RIP and RIP3 kinases, typically referred to as the necrosome. Necroptosis is inhibited by a small molecule inhibitor of RIP, necrostatin-1 (Nec-1) (11). Research studies show that necroptosis contributes to a number of pathological conditions, and Nec-1 has been shown to provide neuroprotection in models such as ischemic brain injury (12). RIP is phosphorylated at several sites within the kinase domain that are sensitive to Nec-1, including Ser14, Ser15, Ser161, and Ser166 (13).\n\u003cb\u003eAlternate Names\u003c\/b\u003e\nAIEFL; Cell death protein RIP; FLJ39204; IMD57; receptor (TNFRSF)-interacting serine-threonine kinase 1; receptor interacting protein; receptor interacting serine\/threonine kinase 1; Receptor-interacting protein 1; receptor-interacting protein kinase 1; Receptor-interacting serine\/threonine-protein kinase 1; RIP; RIP-1; RIP1; RIPK1; Serine\/threonine-protein kinase RIP\n\n\u003cb\u003eSpecification\u003c\/b\u003e\n\nREACTIVITY: H M","brand":"CST","offers":[{"title":"Default Title","offer_id":46800682582185,"sku":"88918V2","price":0.99,"currency_code":"USD","in_stock":true}],"url":"https:\/\/iright.com\/products\/cst-88918v2","provider":"Iright","version":"1.0","type":"link"}