TRAIP Antibody

Code CSB-PA697715
Size US$166
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Image
  • The image on the left is immunohistochemistry of paraffin-embedded Human liver cancer tissue using CSB-PA697715(TRAIP Antibody) at dilution 1/40, on the right is treated with fusion protein. (Original magnification: ×200)
  • The image on the left is immunohistochemistry of paraffin-embedded Human breast cancer tissue using CSB-PA697715(TRAIP Antibody) at dilution 1/40, on the right is treated with fusion protein. (Original magnification: ×200)
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Product Details

Uniprot No.
Target Names
TRAIP
Alternative Names
RING finger protein 206 antibody; RNF206 antibody; TRAF Interacting Protein antibody; TRAF-interacting protein antibody; Traip antibody; TRAIP_HUMAN antibody; TRIP antibody
Raised in
Rabbit
Species Reactivity
Human
Immunogen
Fusion protein of Human TRAIP
Immunogen Species
Homo sapiens (Human)
Conjugate
Non-conjugated
Isotype
IgG
Purification Method
Antigen affinity purification
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
-20°C, pH7.4 PBS, 0.05% NaN3, 40% Glycerol
Form
Liquid
Tested Applications
ELISA,IHC
Recommended Dilution
Application Recommended Dilution
ELISA 1:2000-1:10000
IHC 1:30-1:150
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Background

Function
E3 ubiquitin ligase required to protect genome stability in response to replication stress. Acts as a key regulator of interstrand cross-link repair, which takes place when both strands of duplex DNA are covalently tethered together, thereby blocking replication and transcription. Controls the choice between the two pathways of replication-coupled interstrand-cross-link repair by mediating ubiquitination of MCM7 subunit of the CMG helicase complex. Short ubiquitin chains on MCM7 promote recruitment of DNA glycosylase NEIL3. If the interstrand cross-link cannot be cleaved by NEIL3, the ubiquitin chains continue to grow on MCM7, promoting the unloading of the CMG helicase complex by the VCP/p97 ATPase, enabling the Fanconi anemia DNA repair pathway. Only catalyzes ubiquitination of MCM7 when forks converge. Also involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis: promotes ubiquitination of DPCs, leading to their degradation by the proteasome. Has also been proposed to play a role in promoting translesion synthesis by mediating the assembly of 'Lys-63'-linked poly-ubiquitin chains on the Y-family polymerase POLN in order to facilitate bypass of DNA lesions and preserve genomic integrity. The function in translesion synthesis is however controversial. Acts as a regulator of the spindle assembly checkpoint. Also acts as a negative regulator of innate immune signaling by inhibiting activation of NF-kappa-B mediated by TNF. Negatively regulates TLR3/4- and RIG-I-mediated IRF3 activation and subsequent IFNB1 production and cellular antiviral response by promoting 'Lys-48'-linked polyubiquitination of TNK1 leading to its proteasomal degradation.
Gene References into Functions
  1. The TRAIP coiled-coil domain altered its stoichiometry between dimer and trimer in a concentration-dependent manner. Additionally, the TRAIP RING domain induced even higher-ordered assembly, which was necessary for interacting with the TRAF-N domain of TRAF2 but not TRAF1. PMID: 30127245
  2. TRIP interacts with transforming growth factor beta-activated kinase 1 (TAK1) and promotes K48-linked polyubiquitination of TAK1 in rheumatoid arthritis fibroblast-Like synoviocytes PMID: 27847407
  3. Taken together, these findings improve the understanding clinical implication of TRAIP in various diseases including primordial dwarfism and cancers. PMID: 26820530
  4. cell cycle-dependent transcription of the TRAIP gene by E2F1, E2F2, and E2F4 and rapid protein degradation leads to cell cycle-dependent expression with a maximum in G2/M PMID: 26369285
  5. TRAIP/RNF206 is required for recruitment of RAP80 to sites of DNA damage.( PMID: 26781088
  6. These findings establish TRAIP as a PCNA-binding ubiquitin ligase with an important role in protecting genome integrity after obstacles to DNA replication. PMID: 26711499
  7. 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. PMID: 26595769
  8. The TRAIP ubiquitin ligase activity is functionally required for the spindle assembly checkpoint control. PMID: 25335891
  9. 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 PMID: 26093298
  10. Data indicate that TRAF interacting protein TRIP negatively regulates the TNFR-associated factor 2 (TRAF2) ubiquitin-dependent pathway by modulating the TRAF2-sphingosine 1-phosphate (S1P) interaction. PMID: 25716317
  11. observed enhanced ubiquitylation of Poleta by TRIP E3 ligase and show that TRIP promotes Poleta localization to nuclear foci PMID: 24553286
  12. The TRAF-interacting protein (TRIP) is a regulator of keratinocyte proliferation. PMID: 21068752
  13. CYLD interacts with TRIP and regulates negatively nuclear factor kappaB activation by tumor necrosis factor. PMID: 14676304
  14. The overexpression of TRIP sensitizes cells to TNF-induced apoptosis, an effect that can be reversed by the coexpression of Syk. PMID: 19151749

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Involvement in disease
Seckel syndrome 9 (SCKL9)
Subcellular Location
Nucleus, nucleoplasm. Nucleus, nucleolus. Chromosome. Cytoplasm. Cytoplasm, perinuclear region.
Database Links

HGNC: 30764

OMIM: 605958

KEGG: hsa:10293

STRING: 9606.ENSP00000328203

UniGene: Hs.517972

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