Cat. No. 01-008
Store at -20°C
E. coli RuvA protein binds specifically to the Holliday structure which is the intermediate of recombination at the late stage of homologous recombination and recombination repair and forms a complex with RuvB motor protein allowing the migration of Holliday junction using ATP hydrolysis energy and expands the heteroduplex region. In solution, it forms a tetramer and binds to the cross-like DNA of the Holliday junction from below and above holding it in between (1, 2).
The product is a recombinant protein abundantly expressed by E. coli and purified by methods such as chromatography (Fig. 1). The molecular weight is 22 kD and even in solution, it binds to the Holliday structure and form a tetramer.
- Studies on homologous recombination mechanism.
- For SNP analysis (3).
- Incorporation to DNA circuit.
- Recognition and identification of cross-like DNA.
Purity RuvA protein over 90% by SDS-PAGE (CBB staining)
Concentration 2.7 mg/ml (determined by BCA method)
Form 50% glycerol, 10 mM Tris-HCl (pH7.5), 2 mM EDTA, 100 mM NaCl, 5 mM mercaptoethanol
DataLink UniProtKB/Swiss-Prot P0A809 (RUVA_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 (1992) “Escherichia coli RuvA and RuvB proteins specifically interact with Holliday junctions and promote branch migration.” Genes Dev 6:2214-2220 PMID: 1427081
- Yang Q at al (2003) “Allele-specific Holliday junction formation: a new mechanism of allelic discrimination for SNP scoring.” Genome Research 13:1754-1764 PMID: 12840050