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anti-Human RIPK3 Anticorps:
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Human Polyclonal RIPK3 Primary Antibody pour ELISA, ICC - ABIN4350600
Kaiser, Upton, Mocarski: Receptor-interacting protein homotypic interaction motif-dependent control of NF-kappa B activation via the DNA-dependent activator of IFN regulatory factors. dans Journal of immunology (Baltimore, Md. : 1950) 2008
Show all 34 Pubmed References
Human Polyclonal RIPK3 Primary Antibody pour ICC, IF - ABIN4350602
Davis, Hawkins, Ramasamy, Irrinki, Cameron, Islam, Daswani, Doonan, Manevich, Madesh: Nitration of the mitochondrial complex I subunit NDUFB8 elicits RIP1- and RIP3-mediated necrosis. dans Free radical biology & medicine 2010
Show all 19 Pubmed References
Human Polyclonal RIPK3 Primary Antibody pour WB - ABIN6686545
Qin, Yang, Huang, Du, Mai, Xiao, Lü: Sulforaphane attenuates microglia-mediated neuronal necroptosis through down-regulation of MAPK/NF-κB signaling pathways in LPS-activated BV-2 microglia. dans Pharmacological research 2018
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Human Polyclonal RIPK3 Primary Antibody pour WB - ABIN6146964
Huang, Zheng, Wang, Chen, He, Zhang, Xu, Zhao, Shi, Wang, Zhu, Han: The MLKL Channel in Necroptosis Is an Octamer Formed by Tetramers in a Dyadic Process. dans Molecular and cellular biology 2017
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Human Polyclonal RIPK3 Primary Antibody pour IHC (fro), WB - ABIN537440
Sosna, Voigt, Mathieu, Lange, Thon, Davarnia, Herdegen, Linkermann, Rittger, Chan, Kabelitz, Schütze, Adam: TNF-induced necroptosis and PARP-1-mediated necrosis represent distinct routes to programmed necrotic cell death. dans Cellular and molecular life sciences : CMLS 2014
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Cow (Bovine) Polyclonal RIPK3 Primary Antibody pour IHC, WB - ABIN2777333
Lazrek, Goffard, Schanen, Karquel, Bocket, Lion, Devaux, Hedouin, Gosset, Hober: Detection of hepatitis C virus antibodies and RNA among medicolegal autopsy cases in Northern France. dans Diagnostic microbiology and infectious disease 2006
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Mouse (Murine) Polyclonal RIPK3 Primary Antibody pour IHC (p), WB - ABIN541161
Yu, Huang, Shen, Quast, Chan, Xu, Nolan, Payan, Luo: Identification of RIP3, a RIP-like kinase that activates apoptosis and NFkappaB. dans Current biology : CB 1999
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Mouse (Murine) Polyclonal RIPK3 Primary Antibody pour IHC, ELISA - ABIN1003072
Sun, Lee, Navas, Baldwin, Stewart, Dixit: RIP3, a novel apoptosis-inducing kinase. dans The Journal of biological chemistry 1999
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Study revealed increased kidney expression of RIPK3 in mouse models of progressive kidney fibrosis and in human chronic kidney disease kidney and demonstrate a pathway by which RIPK3 promotes fibrogenesis through the AKT-dependent activation of ATP citrate lyase independently of mixed-lineage kinase domain-like protein-dependent necroptosis.
Study revealed that in kidney tubular epithelial cells RIPK3 promotes oxidative stress and mitochondrial dysfunction by upregulation of NOX4 and inhibition of mitochondrial complex I and -III, and that RIPK3 and NOX4 are critical for kidney tubular injury in vivo. Elevated urinary and plasma RIPK3 levels in human patients with sepsis-induced acute kidney injury represent potential markers of this condition.
Activation of necroptosis by Infleunza A virus leads to the phosphorylation of MLKL by RIPK3 and results in MLKL oligomerization and membrane translocation, leading to membrane disruption and a loss of cellular ion homeostasis.
human polymorphonuclear neutrophils secreted IL-1beta through a previously unrecognized mechanism dependent on RIPK3 and serine proteases but independent of canonical NLRP3 inflammasome and caspase-1 activation.
Ectopic expression of RIP3 promoted cisplatin-induced HepG2/DDP cells death, HMGB1 and LDH release
a signaling circuit involving RIPK3 and PGE2 enhances accumulation and immunosuppressive activity of myeloid-derived suppressor cells
OGT-mediated O-GlcNAcylation of the serine-threonine kinase RIPK3 on threonine 467 (T467) prevented RIPK3-RIPK1 hetero- and RIPK3-RIPK3 homo-interaction.
elevated RIPK3 mRNA levels in peripheral blood mononuclear cells are associated with poor prognosis of acute-on-chronic hepatitis B liver failure.
Ripk3 was involved in microvascular ischemia reperfusion injury via regulation of IP3R-mediated calcium overload, xanthine oxidase-dependent oxidative damage and filopodia-related cellular migration, ultimately leading to endothelial apoptosis and migratory inhibition.
Our data uncover a regulation mechanism of PDC activity, show that pyruvate dehydrogenase complex activation by RIP3 is most likely the major mechanism activated by TNF to increase aerobic respiration and its by-product ROS, and suggest that RIP3-dependent induction of aerobic respiration contributes to pathologies related to oxidative stress
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
PELI1 may function to control inadvertent activation of RIP3, thus preventing aberrant cell death and maintaining cellular homeostasis.
Data indicate that receptor-interacting protein 3 (RIP3) is down-regulated in multiple cancers.
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.
RIPK3-dependent cell death and inflammasome activation in FLT3-internal-tandem-duplication-expressing leukemia-initiating cells
The necroptosis-inducing kinase RIPK3 reduces adipose tissue inflammation and glucose intolerance.
We showed that RIP3 spontaneously drives a necroptosis-induced inflammation in established intestinal cell lines and in ileal/colonic samples from IBD patients.
These data demonstrate that caspase-8 functions in synovial antigen-presenting cells to regulate the response to inflammatory stimuli by controlling RIPK3 action, and this delicate balance maintains homeostasis within the joint.
The induced expression of RIP3 by UHRF1 RNAi depends on the presence of Sp1. Remarkably, the ectopic expression of RIP3 in RIP3-null cancer cells results in a decrease in tumor growth in mice. Therefore, our findings offer insights into RIP3 expression control in cancer cells and suggest an inhibitory effect of RIP3 on tumorigenesis.
2-hydroxyglutarate bound to DNMT1 and stimulated its association with the RIP3 promoter, inducing hypermethylation that reduces RIP3 protein and consequently impaired RIP3-dependent necroptosis.
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.
Study revealed that in kidney tubular epithelial cells RIPK3 promotes oxidative stress and mitochondrial dysfunction by upregulation of NOX4 and inhibition of mitochondrial complex I and -III, and that RIPK3 and NOX4 are critical for kidney tubular injury in vivo. RIPK3 is required for increased mitochondrial translocation of NOX4 in response to proinflammatory stimuli by a mechanism involving protein-protein interaction.
Data suggest that the receptor-interacting protein kinase 3 (RIPK3) kinase domain exhibits catalytically independent function that is important for both RIPK3-dependent necroptosis and apoptosis.
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.
Receptor interacting protein kinase 3 (RIP3) regulates iPSCs generation through modulating cell cycle progression genes.
RIP3 participates in the NLRP3 inflammasome activation in infiltrating macrophages in acute lung injury induced by lipopolysaccharide
the loss of RIPK3 did not alter overall disease outcomes, with deficient animals harboring similar bacterial numbers in the lungs and spleens compared to their wild-type counterparts. Mtb-infected macrophages were not rescued from dying by Ripk3 deletion, nor did this affect production of the pro-inflammatory cytokine IL-1beta, both in vitro and in vivo.
Ripk3 signaling is dispensable to the generation of immunity against herpesvirus infection
this study shows that ZBP1 and RIPK3 induce IRG1 to promote an antiviral metabolic state in neurons
RIPK3 promotes keratinocyte activation and facilitates neutrophil infiltration in the skin independent of necroptosis. These findings may shed new lights on the role of RIPK3 in the skin, and may provide an important clue for the treatment of neutrophil-mediated inflammatory skin diseases, including psoriasis.
Silencing of Ripk3 in cultured motor neurons protected them from toxicity associated with SOD1(G93A) astrocytes. However, constitutive deletion of Ripk3 in Tg SOD1(G93A) mice failed to provide behavioral or neuropathological improvement, demonstrating no similar benefit of Ripk3 silencing in vivo. Lastly, we detected no genotype-specific myelin decompaction, proposed to be a proxy of necroptosis in ALS.
This study showed that RIP3 was highly expressed in DRG, SC and HIP of the sciatic nerve in CCI mice and may be involved in chronic neuroinflammation and neuronecrosis.
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.
Embryonic fibroblasts from RIP3 knockout mice are resistant to necrosis and RIP3 knockout animals are devoid of inflammation inflicted tissue damage in an acute pancreatitis model.
Using an RNA interference screen, the kinase RIP3 was identified as a crucial activator for programmed necrosis induced by TNF and during virus infection; RIP3 regulates necrosis-specific RIP1 phosphorylation.
By comparing the phosphorylation sites in wild-type and RIP3-knockdown L929 cells, 174, 167, and 177 distinct phosphorylation sites were revealed to be dependent on RIP3 at the 0.5, 2, and 4 h time points after TNF treatment, respectively.
The B-Raf(V600E) inhibitor dabrafenib selectively inhibits RIP3 and alleviates acetaminophen-induced liver injury.
RIP3-dependent necroptosis modulates post-ischaemic adverse remodelling in a mouse model of myocardial infarction
The product of this gene is a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases, and contains a C-terminal domain unique from other RIP family members. The encoded protein is predominantly localized to the cytoplasm, and can undergo nucleocytoplasmic shuttling dependent on novel nuclear localization and export signals. It is a component of the tumor necrosis factor (TNF) receptor-I signaling complex, and can induce apoptosis and weakly activate the NF-kappaB transcription factor.
receptor-interacting serine-threonine kinase 3
, receptor-interacting serine/threonine-protein kinase 3-like
, RIP-like protein kinase 3
, receptor interacting protein 3
, receptor-interacting protein 3
, receptor-interacting serine/threonine-protein kinase 3
, homocysteine respondent protein HCYP2