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Human WRN Recombinant Protein (N-His) (HC511012)

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Overview
Catalog No.HC511012
Description
Recombinant Human WRN Protein, N-His (HC511012) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
  • E. coli Expression — High-yield, cost-effective production.
  • High Purity — >90% as determined by SDS-PAGE.
Expression systemE. coli
AccessionQ14191
Protein lengthAsn533-Asp944
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.
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 Names3'-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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Formula
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