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Human RIPK3 Protein expressed in Wheat germ - ABIN1318116
Northington, Chavez-Valdez, Graham, Razdan, Gauda, Martin: Necrostatin decreases oxidative damage, inflammation, and injury after neonatal HI. in Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism 2011
Data identify RIPK3 and the inflammasome as key tumor suppressors in acute myeloid leukemia (show BCL11A Proteins) (AML (show RUNX1 Proteins)).
Results suggest that impaired hepatic proteasome function by alcohol exposure may contribute to hepatic accumulation of RIP3 resulting in necroptosis and steatosis while RIP1 (show UQCRFS1 Proteins) kinase activity is important for alcohol-induced inflammation.
CHIP is a bona fide negative regulator of the RIPK1 (show RIPK1 Proteins)-RIPK3 necrosome formation leading to desensitization of TNF (show TNF Proteins)-mediated necroptosis
CNOT3 (show CNOT3 Proteins) suppression promotes necroptosis by stabilizing mRNAs for cell death-inducing proteins, Ripk1 (show RIPK1 Proteins) and Ripk3.
RIPK3 expression may allow unmasking the necroptotic signalling machinery in melanoma and points to reactivation of this pathway as a treatment option for metastatic melanoma.
Additionally, later in infection, RIP3 is cleaved by the coxsackievirus B3-encoded cysteine protease (show CTSB Proteins) 3C(pro), which serves to abrogate RIP3-mediated necrotic signaling and induce a nonnecrotic form of cell death.
Results identify a crucial role for RIPK3-PGAM5 (show PGAM5 Proteins)-Drp1 (show CRMP1 Proteins)/NFAT (show NFATC1 Proteins) signalling in NKT (show SLC22A6 Proteins) cell activation, and further suggest that RIPK3-PGAM5 (show PGAM5 Proteins) signalling may mediate crosstalk between mitochondrial function and immune signalling.
although JNK (show MAPK8 Proteins) activation and RIP3 expression are induced by FS, neither contributes to the liver injury.
The RIP3 expression is reduced in tumors compared to normal tissue in 85% of breast cancer patients, suggesting that RIP3 deficiency is positively selected during tumor growth/development.
Data implicate the infiltrating macrophages as a source of damaging inflammasomes after photoreceptor detachment in a RIP3-dependent manner and suggest a novel therapeutic target for treatment of retinal diseases.
Results suggest that impaired hepatic proteasome function by alcohol exposure may contribute to hepatic accumulation of RIP3 resulting in necroptosis and steatosis while RIP1 (show RALBP1 Proteins) kinase activity is important for alcohol-induced inflammation.
Study shows that Rip3 mRNA expression is at the highest level in the spleen and duodenum, but lowest level in brain. Protein detection results revealed its localization in different type cells in different tissues that can be either nuclear or cytoplasmic.
we demonstrate that the phosphorylation of Ser345 is not required for the interaction between RIPK3 and MLKL in the necrosome, but is essential for MLKL translocation, accumulation in the plasma membrane, and consequent necroptosis.
Data indicate that receptor-interacting serine-threonine kinase 3 (RIPK3) deletion prevents inflammatory phenotypes in CreLysM (lysozyme (show LYZ Proteins) M) Casp8fl/fl (caspase 8 (show CASP8 Proteins)) mice.
RIP3-induced activation of CaMKII (show CAMK2G Proteins), via phosphorylation or oxidation or both, triggers opening of the mitochondrial permeability transition pore and myocardial necroptosis.
RIPK3 is an essential molecule to maintain the temporal manner of the normal progression of wound closure
deficiency of RIPK3 or MLKL prevents oxalate crystal-induced acute kidney injury.
Results identify a crucial role for RIPK3-PGAM5 (show PGAM5 Proteins)-Drp1 (show CRMP1 Proteins)/NFAT (show NFATC1 Proteins) signalling in NKT (show CTSL1 Proteins) cell activation, and further suggest that RIPK3-PGAM5 (show PGAM5 Proteins) signalling may mediate crosstalk between mitochondrial function and immune signalling.
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