RecA functions in DNA recombination and DNA repair. RecA binds to single stranded DNA, resulting in the polymerization of RecA into a nucleoprotein complex. This complex can align with complementary double stranded DNA, resulting in RecA catalysis of DNA strand exchange. RecA DNA binding is stimulated by ATP hydrolysis or non- hydrolyzable ATP analogs. The RecA-ATP-single stranded DNA complex also can function as a coprotease factor in the proteolytic cleavage of LexA, UmuD and certain bacteriophage proteins. RecA complexed with site-specific oligonucleotides have been used to target and specifically cleave large DNA fragments.
A recombinant E. coli strain overexpressing E. coli recA from a plasmid.
Sold by mass of pure protein determined at OD280 (A280= 0.516 at 1 mg/mL, 1cm).
700 mM Tris-HCl100 mM MgCl250 mM DTTpH 7.6 @ 25 °C
10 mM Tris-HCl1 mM DTT 0.1 mM EDTA 50% glycerolpH 7.5 at 25 °C