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RecA Protein, <i>E. coli</i>
RecA Protein, E. coli

RecA Protein (E. coli) is necessary for genetic recombination, reactions involving DNA repair and UV-induced mutagenesis. RecA promotes the autodigestion of the LexA repressor, UmuD protein and lambda repressor.
 
Name Cat# Size Concentration Price Qty
RecA Protein, E. coli
RPEC-100
1 mg
1 mg/ml
$125.00
RecA Protein, E. coli
RPEC-200
3 mg
1 mg/ml
$200.00
RecA Protein, E. coli
RPEC-OEM
Any Size
please inquire

Description:
RecA Protein (E. coli) is necessary for genetic recombination, reactions involving DNA repair and UV-induced mutagenesis. RecA promotes the autodigestion of the LexA repressor, UmuD protein and lambda repressor. Cleavage of LexA derepresses more than 20 genes (1). In vitro studies indicate that in the presence of ATP, RecA promotes the strand exchange of single-strand DNA fragments with homologous duplex DNA. The reaction has three distinct steps: (i) RecA polymerizes on the single-strand DNA, (ii) the nucleoprotein filament binds the duplex DNA and searches for a homologous region, (iii) the strands are exchanged (2).

Source:
An E. coli strain ER2502 that carries an overexpressed RecA gene from E. coli.

Application:
- Visualization of DNA structures with electron microscopy (3)
- D-loop mutagenesis (4)
- Screening libraries using RecA-coated probes (5,6)
- Cleavage of DNA at any single predetermined site (7,8,9)
- RecA mediated affinity capture for full length cDNA cloning (10, 11)

Supplied in:
10 mM Tris-HCl
1 mM DTT
0.1 mM EDTA
50% Glycerol
pH 7.5 @ 25°C

Supplied with:
10x RecA Reaction Buffer

10x RecA Reaction Buffer:
700 mM Tris-HCl
100 mM MgCl2
50 mM DTT
pH 7.6 @ 25°C

Unit Definition:
Sold by mass of pure protein determined at OD280 (A280 = 0.516 at 1 mg/mL, 1cm).

Recommended Storage Condition: -20°C

References:
1. West, S.C. (1992) Ann. Rev. Biochem., 61, 603-640.
2. Zhumabayeva, B. et al. (1990) Biotechniques, 27, 834-845.
3. Zhumabayeva, B. et al. (2001) Biotechniques, 30, 512-520.
4. Radding, C.M. (1991) J. Biol. Chem., 266, 5355-5358.
5. Wasserman, S.A. and Cozzarelli, N.R. (1985) Proc. Natl. Acad. Sci. USA, 82, 1079-1083.
6. Shortle, D. et al. (1980) Proc. Natl. Acad. Sci. USA, 77, 5375-5379.
7. Honigberg, S.M. et al. (1986) Proc. Natl. Acad. Sci. USA, 83, 9586-9590.
8. Rigas, B. et al. (1986) Proc. Natl. Acad. Sci. USA, 83, 9591-9595.
9. Ferrin, L.J. and Camerini-Otero, R.D. (1991) Science, 254, 1494-1497.
10. Koob, M. et al. (1992) Nucl. Acids Res., 20, 5831-5836.
11. Koob, M. (1992) R. Wu (Eds.), Methods in Enzymology, 216, pp. 321-329. San Diego: Academic Press.

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