Overview

Description

  • Nature
    Recombinant
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species
      Thermus aquaticus
    • Molecular weight
      37 kDa
    • Amino acids
      1 to 340
    • Additional sequence information
      This Protein is from Thermus aquaticus

Specifications

Our Abpromise guarantee covers the use of ab123228 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Biological activity
    The activity of single-stranded DNA-dependent ATPase was confirmed.
  • Applications

    Functional Studies

    SDS-PAGE

    Electron Microscopy

  • Purity
    > 90 % SDS-PAGE.

  • Form
    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at -20°C.

    pH: 8.00
    Constituents: 0.79% Tris HCl, 0.03% EDTA, 50% Glycerol, 1.17% Sodium chloride

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

General Info

  • Alternative names
    • DNA strand exchange and recombination protein with protease and nuclease activity
    • lexB
    • Protein recA
    • recH
    • Recombinase A
    see all
  • Relevance
    RecA 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.
  • Cellular localization
    Cytoplasmic

Images

  • SDS-PAGE of ab123228

References

This product has been referenced in:
  • Shigemori Y  et al. Multiplex PCR: use of heat-stable Thermus thermophilus RecA protein to minimize non-specific PCR products. Nucleic Acids Res 33:e126 (2005). Read more (PubMed: 16087733) »
  • Angov E & Camerini-Otero RD The recA gene from the thermophile Thermus aquaticus YT-1: cloning, expression, and characterization. J Bacteriol 176:1405-12 (1994). Read more (PubMed: 8113181) »

See all 2 Publications for this product

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

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