

| Catalog No. | HC511012 |
|---|---|
| Description |
Recombinant Human WRN Protein, N-His (HC511012) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
|
| Expression system | E. coli |
| Accession | Q14191 |
| Protein length | Asn533-Asp944 |
| 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. |
| 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 | 3'-5' exonuclease, ATP-dependent helicase, Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN, DNA 3'-5' helicase WRN, DNA helicase, RecQ-like type 3, EC:3.1.-.-, EC:5.6.2.4, RECQ3, RECQL2, RecQ protein-like 2, WRN, Werner syndrome protein |
| Background | Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN is a ~162 kDa protein. Multifunctional enzyme that has magnesium and ATP-dependent 3'-5' DNA-helicase activity on partially duplex substrates. Also has 3'->5' exonuclease activity towards double-stranded (ds)DNA with a 5'-overhang. Has no nuclease activity towards single-stranded (ss)DNA or blunt-ended dsDNA. Helicase activity is most efficient with (d)ATP, but (d)CTP will substitute with reduced efficiency; strand displacement is enhanced by single-strand binding-protein (heterotrimeric replication protein A complex, RPA1, RPA2, RPA3). Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. 1. Suzuki, N. et al. (1997) Nucleic acids research 25, 2973-8. PMID: 9224595 2. Gray, MD. et al. (1997) Nature genetics 17, 100-3. PMID: 9288107 3. Shen, JC. et al. (1998) Nucleic acids research 26, 2879-85. PMID: 9611231 4. Xue, Y. et al. (2002) Biochemistry 41, 2901-12. PMID: 11863428 5. Fry, M. et al. (1999) The Journal of biological chemistry 274, 12797-802. PMID: 10212265 |
| Note | For research use only |
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