BellBrook

WRN Helicase (human) (rec.) (His) (active) (1µg)

CHF 441.00
In stock
BBL-2276-C0011 µgCHF 441.00
More Information
Product Details
Synonyms Bifunctional 3'-5' Exonuclease/ATP-dependent Helicase WRN; RecQ Protein-like 2; RECQ3; RECQL2; WRN RecQ-like Helicase
Product Type Protein
Properties
Source/Host Insect cells
Sequence

Recombinant human WRN Helicase enzyme (aa500-946) fused to a N-terminal His-tag.

Crossreactivity Human
Biological Activity

The enzyme has been thoroughly validated with the Transcreener ADP Assay Kit. For specific activity please refer to the Certificate of Analysis for each individual enzyme lot.

MW 51.8kDa
Purity ≥90% (SDS-PAGE)
Accession Number Q14191
Formulation Liquid. In 50mM Tris-HCl pH 8.0, 500mM NaCl, 20% glycerol buffer, 0.5 mM TCEP.
Shipping and Handling
Shipping DRY ICE
Short Term Storage -20°C
Long Term Storage -80°C
Handling Advice Avoid freeze/thaw cycles.
Use/Stability Stable for at least 6 months after receipt when stored at -80°C.
Documents
MSDS Inquire
Product Specification Sheet
Datasheet Download PDF
Description

WRN helicase is a multifunctional enzyme that has both magnesium and ATP-dependent DNA-helicase activity and 3'->5' exonuclease activity towards double-stranded DNA with a 5'-overhang. It has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. It binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. It may play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks, or during DNA repair. It alleviates the stalling of DNA polymerases at the site of DNA lesions and is important for genomic integrity. It plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity) and plays a role in double-strand break repair after gamma-irradiation.

© 2017 Adipogen Life Sciences. Pictures: © 2012 Martin Oeggerli. All Rights Reserved.