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RecA functions in DNA recombination and DNA repair (1,2,3). 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 (4).
Source of ProteinA recombinant E. coli strain overexpressing E. coli recA from a plasmid.
Supplied in10 mM Tris-HCl1 mM DTT0.1 mM EDTA50% glycerolpH 7.5 @ 25°C
Supplied With:B9260 (10X RecA Reaction Buffer)
10X RecA Reaction Buffer (B9260):700 mM Tris-HCl100 mM MgCl250 mM DTTpH 7.6 @ 25°C
Unit DefinitionSold by mass of pure protein determined atOD280 (A280 = 0.516 at 1 mg/mL, 1cm).
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