Recombinant Rabbit monoclonal primary
Recombinant RIP Monoclonal Antibody (ET1701-79)
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A purified.
Cell death protein RIP antibody; FLJ39204 antibody; OTTHUMP00000039163 antibody; Receptor (TNFRSF) interacting serine threonine kinase 1 antibody; receptor interacting protein 1 antibody; Receptor interacting protein antibody; Receptor interacting protein kinase 1 antibody; Receptor interacting serine threonine protein kinase 1 antibody; Receptor TNFRSF interacting serine threonine kinase 1 antibody; Receptor-interacting protein 1 antibody; Receptor-interacting serine/threonine-protein kinase 1 antibody; Rinp antibody; RIP 1 antibody; RIP antibody; Rip-1 antibody; RIP1 antibody; RIPK 1 antibody; Ripk1 antibody; RIPK1_HUMAN antibody; Serine threonine protein kinase RIP antibody; Serine/threonine-protein kinase RIP antibody
Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.
Proteolytically cleaved by CASP8 at Asp-324. Cleavage is crucial for limiting TNF-induced apoptosis, necroptosis and inflammatory response. Cleavage abolishes NF-kappa-B activation and enhances the interaction of TRADD with FADD.; RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation. Phosphorylation of Ser-161 by RIPK3 is necessary for the formation of the necroptosis-inducing complex. Phosphorylation at Ser-25 represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death. Phosphorylated at Ser-320 by MAP3K7 which requires prior ubiquitination with 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2 (By similarity). This phosphorylation positively regulates RIPK1 interaction with RIPK3 to promote necroptosis but negatively regulates RIPK1 kinase activity and its interaction with FADD to mediate apoptosis (By similarity).; Ubiquitinated with 'Lys-11'-, 'Lys-48'-, 'Lys-63'- and linear-linked type ubiquitin. Polyubiquitination with 'Lys-63'-linked chains by TRAF2 induces association with the IKK complex. Deubiquitination of 'Lys-63'-linked chains and polyubiquitination with 'Lys-48'-linked chains by TNFAIP3 leads to RIPK1 proteasomal degradation and consequently down-regulates TNF-alpha-induced NFkappa-B signaling. 'Lys-48'-linked polyubiquitination by RFFL or RNF34 also promotes proteasomal degradation and negatively regulates TNF-alpha-induced NF-kappa-B signaling. Linear polyubiquitinated; the head-to-tail linear polyubiquitination ('Met-1'-linked) is mediated by the LUBAC complex and decreases protein kinase activity. Deubiquitination of linear polyubiquitin by CYLD promotes the kinase activity (By similarity). Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B. Ubiquitinated with 'Lys-63'-linked chains by PELI1. Ubiquitination at Lys-377 with 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2 is essential for its phosphorylation at Ser-320 mediated by MAP3K7 (By similarity). This ubiquitination is required for NF-kB activation, suppresses RIPK1 kinase activity and plays a critical role in preventing cell death during embryonic development (By similarity).
Cytoplasm, Cell membrane.
In contrast to growth factors which promote cell proliferation, FAS ligand (FAS-L) and the tumor necrosis factors (TNFs) rapidly induce apoptosis. Cellular response to FAS-L and TNF is mediated by structurally related receptors containing a conserved "death domain" and belonging to the TNF receptor superfamily. TRADD, FADD and RIP are FAS/TNF-R1 interacting proteins that contain a death domain homologous region (DDH). TRADD (TNF-R1-associated death domain) and FADD (FAS-associated death domain) associate with the death domains of both FAS and TNF-R1 via their DDH regions. Overexpression of TRADD leads to NFkB activation and apoptosis in the absence of TNF. Overexpression of FADD causes apoptosis, which can be blocked by the cow pox protein CrmA, suggesting that FADD lies upstream of ICE and possibly other serine proteases. The receptor interacting protein, RIP, associates with FAS exclusively via its DDH and this association is abrogated in lpr mutants. Unlike TRADD and FADD, RIP contains a putative amino terminal kinase domain.