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Human TRAIP Recombinant Protein (N-GST & C-His) (HP992022)

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Overview
Catalog No.HP992022
Description
Recombinant Human TRAIP Protein, N-GST & C-His (HP992022) expressed in E. coli, spanning Pro2-Asp75. Purity: >90% by SDS-PAGE.
Highlights
  • His-Tagged — N-terminal 6×His tag for IMAC purification.
  • E. coli Expression — High-yield, cost-effective production.
  • High Purity — >90% purity verified by SDS-PAGE.
Expression systemE. coli
AccessionQ9BWF2
Protein lengthPro2-Asp75
ApplicationsELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
SpeciesHomo sapiens (Human)
Nature Recombinant
Endotoxin level Please contact with the lab for this information.
Purity >90% as determined by SDS-PAGE.
Predicted molecular weight 36.73 kDa
Form Lyophilized
Storage buffer Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

Reconstitution Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Shipping In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Alternate NamesE3 ubiquitin-protein ligase TRAIP, EC:2.3.2.27, RING finger protein 206, RNF206, TRAF-interacting protein, TRAIP, TRIP
Background

E3 ubiquitin-protein ligase TRAIP is a ~53 kDa protein. 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.

1. Chapard, C. et al. (2014) Journal of cell science 127, 5149-56. PMID: 25335891
2. Harley, ME. et al. (2016) Nature genetics 48, 36-43. PMID: 26595769
3. Hoffmann, S. et al. (2016) The Journal of cell biology 212, 63-75. PMID: 26711499
4. Soo Lee, N. et al. (2016) Nature communications 7, 10463. PMID: 26781088
5. Feng, W. et al. (2016) Cell discovery 2, 16016. PMID: 27462463
6. Sonneville, R. et al. (2019) eLife 8. PMID: 31545170
7. Wallace, HA. et al. (2014) Development (Cambridge, England) 141, 1332-41. PMID: 24553286
8. Zhang, M. et al. (2012) The Journal of experimental medicine 209, 1703-11. PMID: 22945920
Note For research use only
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