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TRAIP encodes a protein that contains an N-terminal RING finger motif and a putative coiled-coil domain. Zusätzlich bieten wir Ihnen TRAIP Antikörper (51) und TRAIP Kits (2) und viele weitere Produktgruppen zu diesem Protein an.
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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 (zeige E2F1 Proteine), E2F2 (zeige E2F2 Proteine), and E2F4 (zeige E2F4 Proteine) and rapid protein degradation leads to cell cycle-dependent expression with a maximum in G2/M
TRAIP/RNF206 is required for recruitment of RAP80 (zeige UIMC1 Proteine) 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 (zeige TANK Proteine) TRIP negatively regulates the TNFR (zeige TNFRSF1A Proteine)-associated factor 2 (TRAF2 (zeige TRAF2 Proteine)) ubiquitin-dependent pathway by modulating the TRAF2 (zeige TRAF2 Proteine)-sphingosine 1-phosphate (S1P (zeige MBTPS1 Proteine)) interaction.
The TRAF-interacting protein (zeige TANK Proteine) (TRIP) is a regulator of keratinocyte proliferation.
CYLD (zeige CYLD Proteine) interacts with TRIP and regulates negatively nuclear factor kappaB activation by tumor necrosis factor (zeige TNF Proteine).
TRIP as a negative regulator in TLR3 (zeige TLR3 Proteine)/4- and RIG-I (zeige DDX58 Proteine)-triggered antiviral responses and suggested TRIP as a potential target for the intervention of diseases with uncontrolled IFN-beta (zeige IFNB1 Proteine) 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