Recombinant E. coli RNase H protein (ab113149)

Overview

Description

  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • AccessionP0A7Y4
    • SpeciesEscherichia coli
    • Molecular weight20 kDa including tags
    • Amino acids1 to 155
    • TagsHis tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab113149 in the following tested applications.

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

  • Applications

    SDS-PAGE

    Mass Spectrometry

  • Mass spectrometry
    MALDI-TOF
  • Purity> 95 % SDS-PAGE.
    ab113149 was purified using conventional chromatography techniques.
  • FormLiquid
  • Additional notes


  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

    pH: 8.00
    Constituents: 0.32% Tris HCl, 10% Glycerol, 0.04% DTT

General Info

  • Alternative names
    • Ribonuclease H
    • Ribonuclease HI
    • RNase H
    • RNase HI
    • rnhA
    see all
  • RelevanceRNase H from E. coli is an endoribonuclease that specifically hydrolyzes the phosphodiester bonds of RNA in RNA:DNA duplexes to generate products with 3'-hydroxyl and 5'-phosphate ends.1,2,3 RNase H degrades only the RNA component of the DNA-RNA hybrid (RNA that is hydrogen bonded to a complementary DNA strand). Other enzymes in E. coli which degrade RNA in the DNA-RNA hybrid are DNA polymerase I and exonuclease III, but these degrade either the RNA or DNA of the hybrids. Ribonuclease H will not cleave single-stranded or double-stranded DNA or RNA.1,2
  • Cellular localizationCytoplasmic

Recombinant E. coli RNase H protein images

  • 15% SDS-PAGE showing ab113149 (3 µg) at approximately 20 kDa.

References for Recombinant E. coli RNase H protein (ab113149)

ab113149 has not yet been referenced specifically in any publications.

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