Key features and details
- Expression system: Escherichia coli
- Purity: > 90% SDS-PAGE
- Suitable for: Functional Studies, SDS-PAGE, Electron Microscopy
Product nameRecombinant E. coli RecA protein (Active)
See all RecA proteins and peptides
Purity> 90 % SDS-PAGE.
ab174091 was over-expressed as a recombinant protein and highly purified by several steps of chromatography.
Expression systemEscherichia coli
Protein lengthFull length protein
SequenceMAIDENKQKALAAALGQIEKQFGKGSIMRLGEDRSMDVETISTGSLSLDI ALGAGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGKTCAFIDAEHAL DPIYARKLGVDIDNLLCSQPDTGEQALEICDALARSGAVDVIVVDSVAAL TPKAEIEGEIGDSHMGLAARMMSQAMRKLAGNLKQSNTLLIFINQIRMKI GVMFGNPETTTGGNALKFYASVRLDIRRIGAVKEGENVVGSETRVKVVKN KIAAPFKQAEFQILYGEGINFYGELVDLGVKEKLIEKAGAWYSYKGEKIG QGKANATAWLKDNPETAKEIEKKVRELLLSNPNSTPDFSVDDSEGVAETN EDF
Predicted molecular weight36 kDa
Amino acids1 to 353
Our Abpromise guarantee covers the use of ab174091 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Store at -20°C long term. Avoid freeze / thaw cycle.
Constituents: 50% Glycerol (glycerin, glycerine), 0.32% Tris-HCl buffer, 0.03% EDTA, 1.1% Potassium chloride, 0.02% DTT
- DNA strand exchange and recombination protein with protease and nuclease activity
- Protein recA
RelevanceRecA in E.coli can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with lexA causing its activation and leading to its autocatalytic cleavage.
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab174091 has been referenced in 1 publication.
- Horii T et al. Regulation of SOS functions: purification of E. coli LexA protein and determination of its specific site cleaved by the RecA protein. Cell 27:515-22 (1981). Functional Studies ; Escherichia coli . PubMed: 6101204