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anti-Human RIPK3 Antibodies:
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Human Polyclonal RIPK3 Primary Antibody for 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. in Journal of immunology (Baltimore, Md. : 1950) 2008
Show all 22 Pubmed References
Human Polyclonal RIPK3 Primary Antibody for 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. in Free radical biology & medicine 2010
Show all 16 Pubmed References
Human Polyclonal RIPK3 Primary Antibody for IHC (p), WB - ABIN392275
Sun, Lee, Navas, Baldwin, Stewart, Dixit: RIP3, a novel apoptosis-inducing kinase. in The Journal of biological chemistry 1999
Show all 5 Pubmed References
Mouse (Murine) Polyclonal RIPK3 Primary Antibody for IHC, ELISA - ABIN1003072
Yu, Huang, Shen, Quast, Chan, Xu, Nolan, Payan, Luo: Identification of RIP3, a RIP-like kinase that activates apoptosis and NFkappaB. in Current biology : CB 1999
Show all 3 Pubmed References
Cow (Bovine) Polyclonal RIPK3 Primary Antibody for 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. in Diagnostic microbiology and infectious disease 2006
Show all 2 Pubmed References
Human Polyclonal RIPK3 Primary Antibody for IHC (p), WB - ABIN391272
Viringipurampeer, Ferreira, DeMaria, Yoon, Shan, Moosajee, Gregory-Evans, Ngai, Gregory-Evans: Pax2 regulates a fadd-dependent molecular switch that drives tissue fusion during eye development. in Human molecular genetics 2012
Mouse (Murine) Polyclonal RIPK3 Primary Antibody for IHC, WB - ABIN4350598
Gilley, González-Juarbe, Shenoy, Reyes, Dube, Restrepo, Orihuela: Infiltrated Macrophages Die of Pneumolysin-Mediated Necroptosis following Pneumococcal Myocardial Invasion. in Infection and immunity 2016
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 (show CASP8 Antibodies) 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 (show UHRF1 Antibodies) RNAi depends on the presence of Sp1 (show PSG1 Antibodies). 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 (show DNMT1 Antibodies) and stimulated its association with the RIP3 promoter, inducing hypermethylation that reduces RIP3 protein and consequently impaired RIP3-dependent necroptosis.
the in vivo effects were diametrically reversed with RIP3 deletion or RIP1 (show UQCRFS1 Antibodies) blockade, resulting in marked tumor protection. The dichotomy between the in vivo and in vitro results suggests that the microenvironmental milieu resulting from RIP1 (show UQCRFS1 Antibodies)/RIP3 signaling is likely responsible for its protumorigenic effects
Shikonin induces glioma cell necroptosis in vitro by reactive oxygen species overproduction and promoting RIP1 (show UQCRFS1 Antibodies)/RIP3 necrosome formation.
In critically ill trauma patients, plasma levels of the necroptosis mediator RIP3 at 48 h were associated with AKI stage and RBC (show CACNA1C Antibodies) transfusions.
our results reveal that the necroptosis adaptor RIPK3 has key anti-inflammatory and anti-tumoral functions in the intestine, and define RIPK3 as a novel colon tumor suppressor
adhesion-induced eosinophil cytolysis takes place through RIPK3-MLKL-dependent necroptosis, which can be counterregulated by autophagy
RIP3 (show MPRIP Antibodies)-mediated signaling is not a critical driver of acute radiation syndrome
RIPK3 promotes adenovirus type 5 oncolytic activity.
p55TNFR-IKK2 (show IKBKB Antibodies)-Ripk3 signalling orchestrates arthritogenic and death responses in synovial fibroblasts
in Mycobacterium tuberculosis-infected macrophages, mitochondria are an essential platform for induction of necrosis by activating RIPK3 function and preventing caspase 8 (show CASP8 Antibodies)-activation.
Ripk3 promotes mitochondrial apoptosis via inhibition of FUNDC1 (show FUNDC1 Antibodies) mitophagy in cardiac ischemia reperfusion injury.
The authors report here that male reproductive organs of both Ripk3- and Mlkl-knockout mice retain 'youthful' morphology and function into advanced age, while those of age-matched wild-type mice deteriorate. Feeding of wild-type mice with an RIPK1 (show RIPK1 Antibodies) inhibitor prior to the normal onset of age-related changes in their reproductive organs blocked the appearance of signs of aging.
These data demonstrate a role for RIP3 (show MPRIP Antibodies) in promoting in vivo thrombosis and hemostasis by amplifying platelet activation. RIP3 (show MPRIP Antibodies) may represent a novel promising therapeutic target for thrombotic diseases.
these results demonstrated that RIPK3-mediated signaling in Tie-2 expressing cells was responsible for the embryonic lethality of Fadd-/- with cardiac failure.
Pull down experiments with biotinylated Sorafenib show that it binds independently RIPK1 (show RIPK1 Antibodies), RIPK3 and MLKL. Moreover, it inhibits RIPK1 (show RIPK1 Antibodies) and RIPK3 kinase activity. In vivo Sorafenib protects against TNF (show TNF Antibodies)-induced systemic inflammatory response syndrome (SIRS) and renal ischemia-reperfusion injury (IRI).
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