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Taq RecA (Active) Protein

Origin: Thermus aquaticus Host: Escherichia coli (E. coli) Recombinant > 90 % of protein determined by SDS-PAGE (CBB staining) Func Active
Catalog No. ABIN2452211
  • Target
    Taq RecA
    Protein Type
    Recombinant
    Biological Activity
    Active
    Origin
    Thermus aquaticus
    Source
    Escherichia coli (E. coli)
    Application
    Functional Studies (Func)
    Characteristics
    Single-strand dependent ATPase activity. The activity of single-stranded DNA-dependent ATPase was confirmed.
    Purity
    > 90 % of protein determined by SDS-PAGE (CBB staining)
  • Application Notes
    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.
    Restrictions
    For Research Use only
  • Format
    Liquid
    Concentration
    1 mg/mL
    Buffer
    50 mM Tris-HCl ( pH 8.0), 200 mM NaCl, 1 mM EDTA, 50 % glycerol
    Storage
    -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
    Background
    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.
    UniProt
    P48296
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