抗Human RIPK1 抗体:
抗Mouse (Murine) RIPK1 抗体:
抗Rat (Rattus) RIPK1 抗体:
Human Polyclonal RIPK1 Primary Antibody for ELISA, ICC - ABIN4350584
Nilsson, Loganathan, Sekiguchi, Matsuba, Hui, Tsubuki, Tanaka, Iwata, Saito, Saido: Aβ secretion and plaque formation depend on autophagy. in Cell reports 2013
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Human Monoclonal RIPK1 Primary Antibody for IP, WB - ABIN532716
Festjens, Vanden Berghe, Cornelis, Vandenabeele: RIP1, a kinase on the crossroads of a cell's decision to live or die. in Cell death and differentiation 2007
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Human Polyclonal RIPK1 Primary Antibody for WB - ABIN3042930
Chen, Zhao, Wu, Zou, Luo, Li, Xie, Liang: The role of RIP1 and RIP3 in the development of aplastic anemia induced by cyclophosphamide and busulphan in mice. in International journal of clinical and experimental pathology 2015
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Human Polyclonal RIPK1 Primary Antibody for WB - ABIN3042480
Wang, Ma, Hu, Xie, Wu, Zeng, Song: Bifidobacterial recombinant thymidine kinase-ganciclovir gene therapy system induces FasL and TNFR2 mediated antitumor apoptosis in solid tumors. in BMC cancer 2017
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Human Polyclonal RIPK1 Primary Antibody for IF (p), IHC (p) - ABIN715016
Luo, Roy, Xiao, Sun, Liang, Chen, Fu, Sun, Zhu, Ye, Liu: Lycorine induces programmed necrosis in the multiple myeloma cell line ARH-77. in Tumour biology 2014
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Human Polyclonal RIPK1 Primary Antibody for IF (p) - ABIN715023
Seifert, Werba, Tiwari, Giao Ly, Alothman, Alqunaibit, Avanzi, Barilla, Daley, Greco, Torres-Hernandez, Pergamo, Ochi, Zambirinis, Pansari, Rendon, Tippens, Hundeyin, Mani, Hajdu, Engle, Miller: The necrosome promotes pancreatic oncogenesis via CXCL1 and Mincle-induced immune suppression. in Nature 2016
Human Polyclonal RIPK1 Primary Antibody for IHC, IHC (p) - ABIN4350581
Ratovitski: Phospho-ΔNp63α-responsive microRNAs contribute to the regulation of necroptosis in squamous cell carcinoma upon cisplatin exposure. in FEBS letters 2015
Human Polyclonal RIPK1 Primary Antibody for ICC, IF - ABIN4350585
Hirsch, von der Wall, Hummel, Dürkop: RIP1 expression is necessary for CD30-mediated cell death induction in anaplastic large-cell lymphoma cells. in Laboratory investigation; a journal of technical methods and pathology 2013
RIP1 was upregulated and contributed to both intrinsic and acquired resistance of melanoma cells to BRAF/MEK inhibitors through activation of NF-kappaB.
RIPK1 turned out to be essential for poly(I:C)/TWEAK-induced caspase-8-mediated apoptosis.
TAK1, receptor-interacting kinase 1 (RIPK1) as well as canonical and non-canonical NF-kappaB signaling are differentially involved in SM-induced cell death in breast cancer cells.
Tozasertib not only targets Aurora kinases but also RIPK1 independently, and that we could generate analogues with increased selectivity to RIPK1 or Aurora kinases, respectively
The MK2 phosphorylates a cytoplasmic pool of RIPK1 that presumably subsequently integrates complex I, while IKKalpha/beta phosphorylate RIPK1 directly in complex I.
This paper describes RIP1 as a checkpoint kinase governing tumor immunity.
The ubiquitination site of RIPK1 (RIPK1-K377) was critical for this interaction with MCU.
Polo-like kinase 1 is recruited into mitotic ripoptosomes, where PLK1's activity is controlled via RIPK1-dependent recruitment and Caspase-8-mediated cleavage, ensuring chromosome stability and faithful chromosome segregation during mitosis.
Molecular modeling/simulation coupled with site-directed mutagenesis revealed that Asp(147) or Asn(169) of RIPK1 are key for ceramide binding and that Arg(258) or Leu(293) residues are involved in the nonmuscle myosin heavy chain II-A interaction, leading to ceramidosome formation and necroptosis.
TANK-binding kinase 1 protein (TBK1) and IKK-epsilon protein (IKKepsilon) phosphorylate the kinase receptor (TNFRSF)-interacting serine-threonine kinase 1 (RIPK1) and prevent RIPK1-dependent cell death.
Point mutations E626K, M637K, and S657K in RIP1 Death Domain exhibit dominant negative effects on RIPoptosome complex formation.
RIPK1 activation during extracellular matrix detachment results in mitophagy induction through a mechanism dependent on the mitochondrial phosphatase PGAM5. As a consequence of mitophagy, ECM-detached cells experience diminished NADPH production in the mitochondria, and the subsequent elevation in ROS levels leads to non-apoptotic death.
REVIEW: recent structural studies of the core machinery of the pathway, the protein kinases receptor-interacting protein kinase (RIPK)1 and RIPK3, and the terminal effector, the pseudokinase mixed lineage kinase domain-like protein (MLKL), in shaping our mechanistic understanding of necroptotic signaling
Depletion of human IKK1, IKK2 or IKK1/2 leads to strongly impaired NF-kappaB activation. Only IKK1/2 double-deficient cells are sensitized to TNF-alpha induced cell death. Cell death is mediated independently on NF-kappaB via RIPK1.
The characterization of RIPK1-deficient patients highlights the essential role of RIPK1 in controlling human immune and intestinal homeostasis, and might have critical implications for therapies targeting RIPK1.
Through driving a feedforward signaling axis of ACTN4-RIPK1-NF-kappaB.
Data indicate that Hsp70 plays a previously unrecognized and important role in suppressing RIP1 activity.
The caspase 8 mediated RIPK1 cleavage product has a pro-apoptotic function, and further cleavage of this pro-apoptotic cleavage product by human rhinovirus 3C protease may provide a mechanism by which human rhinovirus limits apoptosis.
The major function of RIP1 kinase activity in TNF-induced necroptosis is to autophosphorylate serine 161. This specific phosphorylation then enables RIP1 to recruit RIP3 and form a functional necrosome, a central controller of necroptosis.
In lesional psoriatic epidermis, RIPK1-expression was decreased compared with that in normal epidermis. RIPK1-knockdown enhanced TRAIL-mediated expression of psoriasis-relating cytokines in normal human epidermal keratinocytes.
These data suggest that lysosomal dysfunction after spinal cord injury may contribute to both inhibition of autophagy and sensitize cells to necroptosis by promoting RIPK1 and RIPK3 accumulation.
Triad3a promotes the negative feedback loop independently of typical RipK1 ubiquitin editing enzymes
Parkin modulates the lysine 63 ubiquitination status of RIPK1 to promote the activation of NF-kappaB and MAPKs.
These findings indicate that the triggering of inflammation by Casp8 deletion in mice occurs, in part, independently of necroptosis or other functions of RIPK3, and rather reflects enhanced RIPK1-dependent signaling for activation of inflammatory genes.
RIP kinase 1-dependent endothelial necroptosis underlies systemic inflammatory response syndrome.
Increased Ripk1-mediated bone marrow necroptosis is associated with myelodysplasia and bone marrow failure.
Data show that IkappaB kinase (IKK) controlled thymocyte survival by repressing cell-death-inducing activity of the serine/threonine kinase RIPK1 (RIPK1).
our data demonstrate the protective role of RIPK1 downstream of Fas and highlight the general protective function of RIPK1 in hepatocytes exposed to inflammatory conditions, where TNF-alpha, FasL and/or TRAIL are present.
This study showed that RIP1 was highly expressed in DRG, SC and HIP of the sciatic nerve in CCI mice and may be involved in chronic neuroinflammation and neuronecrosis.
It has been proposed that ABIN-1 provides a critical link between methionine1 ubiquitylation mediated by the LUBAC complex and lysine63 deubiquitylation by phospho-A20 to modulate the activation of RIPK1.
Receptor-Interacting Protein Kinases 1 and 3, and Mixed Lineage Kinase Domain-Like Protein Are Activated by Sublytic Complement and Participate in Complement-Dependent Cytotoxicity.
Differentiation of macrophages increased the expression of pro-inflammatory cytokines but reduced RipK1-dependent cell death and the RipK3-caspase-8 interaction. The expression of the anti-apoptotic mediators, X-linked inhibitor of apoptosis protein (XIAP) and caspase-like apoptosis regulatory protein (cFLIPL), also increased in differentiated macrophages, which inhibited caspase activation.
necroptosis contributes to ischemic brain injury induced by oxygen-glucose deprivation and middle cerebral artery occlusion and implicate HIF-1alpha, RIP1, RIP3, and MLKL in necroptosis.
miR-155 up-regulation in macrophages by Salmonella infection causes macrophage death and it may be mediated by both RIP1/3-related necroptosis and PARP-1-mediated necrosis.
Ischemia induces an up-regulation of RIP1K and an enhancement of RIP1K-RIP3K complex formation in neurons and astrocytes. Inhibition of RIP1K increases ischemia-induced reduction in MAP2 or GFAP and decreases ischemia-induced neuronal or astrocytic cell necrosis in the ischemic cortex, and directly protects OGD-induced neuronal or astrocytic cell death. Nec-1 blocks RIP1K-RIP3K complex formation.
Aldehyde dehydrogenase 2 deficiency negates chronic low-to-moderate alcohol consumption-induced cardioprotecion possibly via ROS-dependent apoptosis and RIP1/RIP3/MLKL-mediated necroptosis.
Elevated A20 promotes TNF-induced and RIPK1-dependent intestinal epithelial cell death
Our results reveal a critical role of the RIPK1/DRP1 signaling axis, whose activation leads to mitochondrial fission and ROS release, in modulating porcine NLRP3 inflammasome-mediated IL-1beta production in swine influenza virus-infected porcine alveolar macrophages.
Interaction of xFADD and xRIP1 induced synergistic activation of JNK and NF-kappaB.
Serine-threonine kinase which transduces inflammatory and cell-death signals (necroptosis) following death receptors ligation, activation of pathogen recognition receptors (PRRs), and DNA damage. Upon activation of TNFR1 by the TNF-alpha family cytokines, TRADD and TRAF2 are recruited to the receptor. Ubiquitination by TRAF2 via 'Lys-63'-link chains acts as a critical enhancer of communication with downstream signal transducers in the mitogen-activated protein kinase pathway and the NF-kappa-B pathway, which in turn mediate downstream events including the activation of genes encoding inflammatory molecules. Polyubiquitinated protein binds to IKBKG/NEMO, the regulatory subunit of the IKK complex, a critical event for NF-kappa-B activation. Interaction with other cellular RHIM-containing adapters initiates gene activation and cell death. RIPK1 and RIPK3 association, in particular, forms a necroptosis-inducing complex.
, cell death protein RIP
, receptor interacting protein
, receptor-interacting protein 1
, receptor-interacting serine/threonine-protein kinase 1
, serine/threonine-protein kinase RIP
, receptor (TNFRSF)-interacting serine-threonine kinase 1
, receptor interacting serine/threonine kinase 1 L homeolog
, receptor-interacting protein 1 beta