Cat. No. 01-012
Store at -20°C
E. coli RuvC protein is a structurally specific endonuclease which binds specifically to the Holliday structure, an intermediate of recombination, at the late stage of homologous recombination and recombination repair and introduces a nick in the symmetrical point of the Holliday junction cleaving and resolving the recombinant (1, 2). The product is a recombinant protein abundantly expressed by E. coli and purified by methods such as chromatography (Fig. 1). Its molecular weight is 19 kD and forms a dimer in liquid and in binding state with the Holliday structure.
- Studies on homologous recombination mechanism
- To use as endonuclease which functions specifically to the Holliday structure
Purity: RuvC protein over 90% by SDS-PAGE (CBB staining)
Concentration: 1.0 mg/ml (determined by BCA method)
Form: 50% glycerol, 10 mM Tris-HCl (pH7.5), 2 mM EDTA, 100 mM NaCl, 5 mM mercaptoethanol
Data Link UniProtKB/Swiss-Prot P0A814 (RUVC_ECOLI)
- Shinagawa H and Iwasaki H (1996) “Processing the holliday junction in homologous recombination.” Trend Biochem Sci 21:107-111 PMID: 8882584
- Iwasaki H et al (1991) “Escherichia coli RuvC protein is an endonuclease that resolves the Holliday structure.” EMBO J 10:4381-4389 (1991) PMID: 1661673
- Murayama Y et al (2008) “Formation and branch migration of Holliday junctions mediated by eukaryotic recombinases.”Nature 451:1018-1021PMID:18256600
*This product was used in References 2 and 3.