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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 Proteins (3) and TRAIP Kits (2) and many more products for this protein.
Showing 10 out of 53 products:
Human Polyclonal TRAIP Primary Antibody for IHC (p), WB - ABIN389323
Wu, Ma, Brown, Geisler, Li, Tzeng, Jia, Jurisica, Li: Systematic identification of SH3 domain-mediated human protein-protein interactions by peptide array target screening. in Proteomics 2007
Show all 2 references for ABIN389323
Human Polyclonal TRAIP Primary Antibody for EIA, IHC (p) - ABIN357988
Regamey, Hohl, Liu, Roger, Kogerman, Toftgard, Huber: The tumor suppressor CYLD interacts with TRIP and regulates negatively nuclear factor kappaB activation by tumor necrosis factor. in The Journal of experimental medicine 2003
Show all 2 references for ABIN357988
Human Polyclonal TRAIP Primary Antibody for IHC, ELISA - ABIN184988
Lee, Lee, Choi: TRAF-interacting protein (TRIP): a novel component of the tumor necrosis factor receptor (TNFR)- and CD30-TRAF signaling complexes that inhibits TRAF2-mediated NF-kappaB activation. in The Journal of experimental medicine 1997
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 Antibodies), E2F2 (show E2F2 Antibodies), and E2F4 (show E2F4 Antibodies) 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 Antibodies) 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 Antibodies) TRIP negatively regulates the TNFR (show TNFRSF1A Antibodies)-associated factor 2 (TRAF2 (show TRAF2 Antibodies)) ubiquitin-dependent pathway by modulating the TRAF2 (show TRAF2 Antibodies)-sphingosine 1-phosphate (S1P (show MBTPS1 Antibodies)) interaction.
The TRAF-interacting protein (show TANK Antibodies) (TRIP) is a regulator of keratinocyte proliferation.
CYLD (show CYLD Antibodies) interacts with TRIP and regulates negatively nuclear factor kappaB activation by tumor necrosis factor (show TNF Antibodies).
TRIP as a negative regulator in TLR3 (show TLR3 Antibodies)/4- and RIG-I (show DDX58 Antibodies)-triggered antiviral responses and suggested TRIP as a potential target for the intervention of diseases with uncontrolled IFN-beta (show IFNB1 Antibodies) 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