

| Catalog No. | HD168012 |
|---|---|
| Description |
Recombinant Human ERCC6 Protein, N-His (HD168012) expressed in E. coli, spanning Gly456-Arg745. Purity: >90% by SDS-PAGE.
Highlights
|
| Expression system | E. coli |
| Accession | Q03468 |
| Protein length | Gly456-Arg745 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Species | Homo sapiens (Human) |
| Nature | Recombinant |
| Endotoxin level | Please contact with the lab for this information. |
| Purity | >90% as determined by SDS-PAGE. |
| Predicted molecular weight | 36.12 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 Names | ATP-dependent helicase ERCC6, CSB, Cockayne syndrome protein CSB, DNA excision repair protein ERCC-6, EC:3.6.4.-, ERCC6 |
| Background | DNA excision repair protein ERCC-6 is a ~168 kDa protein. Essential factor involved in transcription-coupled nucleotide excision repair (TC-NER), a process during which RNA polymerase II-blocking lesions are rapidly removed from the transcribed strand of active genes. Plays a central role in the initiation of the TC-NER process: specifically recognizes and binds RNA polymerase II stalled at a lesion, and mediates recruitment of ERCC8/CSA, initiating DNA damage excision by TFIIH recruitment. Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA. Acts as a chromatin remodeler at DSBs; DNA-dependent ATPase-dependent activity is essential for this function. Plays an important role in regulating the choice of the DNA double-strand breaks (DSBs) repair pathway and G2/M checkpoint activation; DNA-dependent ATPase activity is essential for this function. 1. Sarker, AH. et al. (2005) Molecular cell 20, 187-98. PMID: 16246722 2. Anindya, R. et al. (2010) Molecular cell 38, 637-48. PMID: 20541997 3. Bailey, AD. et al. (2012) DNA repair 11, 488-501. PMID: 22483866 4. Sin, Y. et al. (2016) The Journal of biological chemistry 291, 1387-97. PMID: 26620705 5. van der Weegen, Y. et al. (2020) Nature communications 11, 2104. PMID: 32355176 6. Kokic, G. et al. (2021) Nature 598, 368-372. PMID: 34526721 7. Kokic, G. et al. (2024) Nature structural & molecular biology 31, 536-547. PMID: 38316879 8. Carnie, CJ. et al. (2024) Nature cell biology 26, 797-810. PMID: 38600235 9. van Sluis, M. et al. (2024) Nature cell biology 26, 770-783. PMID: 38600236 |
| Note | For research use only |
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