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TRAIP encodes a protein that contains an N-terminal RING finger motif and a putative coiled-coil domain. Additionally we are shipping TRAIP Antibodies (52) and TRAIP Proteins (3) and many more products for this protein.
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Taken together, these findings improve the understanding clinical implication of TRAIP in various diseases including primordial dwarfism and cancers.
cell cycle-dependent transcription of the TRAIP gene by E2F1 (show E2F1 ELISA Kits), E2F2 (show E2F2 ELISA Kits), and E2F4 (show E2F4 ELISA Kits) and rapid protein degradation leads to cell cycle-dependent expression with a maximum in G2/M
TRAIP/RNF206 is required for recruitment of RAP80 (show UIMC1 ELISA Kits) to sites of DNA damage.(
These findings establish TRAIP as a PCNA-binding ubiquitin ligase with an important role in protecting genome integrity after obstacles to DNA replication.
TRAIP is a component of the DNA damage response to replication-blocking DNA lesions.TRAIP promotes DNA damage response during genome replication and is mutated in primordial dwarfism.
The TRAIP ubiquitin ligase activity is functionally required for the spindle assembly checkpoint control.
a number of TRAIP mutants were used to define the TRAIP molecular domains responsible for its homo-dimerization. A co-immunoprecipitation assay indicated that the TRAIP forms homo-dimerization through the CC domain
Data indicate that TRAF interacting protein (show TANK ELISA Kits) TRIP negatively regulates the TNFR (show TNFRSF1A ELISA Kits)-associated factor 2 (TRAF2 (show TRAF2 ELISA Kits)) ubiquitin-dependent pathway by modulating the TRAF2 (show TRAF2 ELISA Kits)-sphingosine 1-phosphate (S1P (show MBTPS1 ELISA Kits)) interaction.
The TRAF-interacting protein (show TANK ELISA Kits) (TRIP) is a regulator of keratinocyte proliferation.
CYLD (show CYLD ELISA Kits) interacts with TRIP and regulates negatively nuclear factor kappaB activation by tumor necrosis factor (show TNF ELISA Kits).
TRIP as a negative regulator in TLR3 (show TLR3 ELISA Kits)/4- and RIG-I (show DDX58 ELISA Kits)-triggered antiviral responses and suggested TRIP as a potential target for the intervention of diseases with uncontrolled IFN-beta (show IFNB1 ELISA Kits) production.
This gene encodes a protein that contains an N-terminal RING finger motif and a putative coiled-coil domain. A similar murine protein interacts with TNFR-associated factor 1 (TRAF1), TNFR-associated factor 2 (TRAF2), and cylindromatosis. The interaction with TRAF2 inhibits TRAF2-mediated nuclear factor kappa-B, subunit 1 activation that is required for cell activation and protection against apoptosis.
, TRAF interacting protein
, ring finger protein 206