Single-strand dependent ATPase activity. The activity of single-stranded DNA-dependent ATPase was confirmed.
Reinheit
> 90 % of protein determined by SDS-PAGE (CBB staining)
Applikationshinweise
1) Useful for studying homologous recombination 2) Increase the specificity and yield of multiplex PCR (of cDNA or genomic DNA) by promoting homologous annealing of primers to target DNA 3) Visualization of DNA with electoron microscopy due to nucleofilament formation.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Konzentration
1 mg/mL
Buffer
50 mM Tris-HCl ( pH 8.0), 200 mM NaCl, 1 mM EDTA, 50 % glycerol
Lagerung
-20 °C
Shigemori, Mikawa, Shibata, Oishi: "Multiplex PCR: use of heat-stable Thermus thermophilus RecA protein to minimize non-specific PCR products." in: Nucleic acids research, Vol. 33, Issue 14, pp. e126, (2005) (PubMed).
Angov, Camerini-Otero: "The recA gene from the thermophile Thermus aquaticus YT-1: cloning, expression, and characterization." in: Journal of bacteriology, Vol. 176, Issue 5, pp. 1405-12, (1994) (PubMed).
Target
Taq RecA
Hintergrund
Thermus aquaticus RecA protein is a thermostable enzyme which plays important roles in homologous recombination and DNA repair. This protein has activities of single-stranded DNA dependent ATPase, DNA annealing, and exchanging of strands between two recombining DNA double helices, similar to E.coli RecA protein, but the optimal temperature is between 65~75 °C. Taq RecA was expressed in E.coli in large quantities and the protein was highly purified. MW is 36.5kD.