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. Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. 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. Alleviates stalling of DNA polymerases at the site of DNA lesions. Important for genomic integrity. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity). Plays a role in double-strand break repair after gamma-irradiation.
Background References
1. Lebel M. et. al. Werner syndrome (WRN) gene variants and their association with altered function and age-associated diseases. Ageing Res Rev. 2018 Jan;41:82-97.
2. Orlovetskie N. et. al. Targeted inhibition of WRN helicase, replication stress and cancer. Biochim Biophys Acta Rev Cancer. 2017 Jan;1867(1):42-48.
Western blot analysis of WRN on different lysates with Rabbit anti-WRN antibody (ET7110-26) at 1/1,000 dilution.
Lane 1: HeLa cell lysate Lane 2: Jurkat cell lysate Lane 3: K-562 cell lysate
Lysates/proteins at 30 µg/Lane.
Predicted band size: 162 kDa Observed band size: 162 kDa
Exposure time: 1 minute; ECL: K1801;
4-20% SDS-PAGE gel.
Proteins were transferred to a PVDF membrane and blocked with 5% NFDM/TBST for 1 hour at room temperature. The primary antibody (ET7110-26) at 1/1,000 dilution was used in 5% NFDM/TBST at 4℃ overnight. Goat Anti-Rabbit IgG - HRP Secondary Antibody (HA1001) at 1/50,000 dilution was used for 1 hour at room temperature.
☑ Knockdown (KD)
Species: Human
Cell sample: HeLa
Antibody concentration: 1: 1000
Data by conrtesy of: Mr. Haihua Xie, School of Basic Medical Sicences, Zhejiang University
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