Recombinant Human Carbonic Anhydrase I protein (ab89359)

Overview

Description

  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • SpeciesHuman

Specifications

Our Abpromise guarantee covers the use of ab89359 in the following tested applications.

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

  • Applications

    Western blot

    SDS-PAGE

  • Purity> 95 % SDS-PAGE.
    ab89359 is purified using conventional chromatography techniques.
  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

    Preservative: None
    Constituents: 10% Glycerol, 20mM Tris HCl, 1mM DTT, pH 8.0

General Info

  • Alternative names
    • CA 1
    • CA I
    • CA-I
    • CA1
    • CAB
    • CAH1_HUMAN
    • CAI
    • CAN
    • Car 1
    • Car1
    • Carbonate dehydratase I
    • Carbonic anhydrase 1
    • Carbonic anhydrase A
    • Carbonic anhydrase B
    • Carbonic anhydrase B, formerly
    • Carbonic anhydrase I
    • Carbonic dehydratase
    • ECK0125
    • JW0122
    • yadF
    see all
  • FunctionReversible hydration of carbon dioxide. Can hydrates cyanamide to urea.
  • Sequence similaritiesBelongs to the alpha-carbonic anhydrase family.
  • Cellular localizationCytoplasm.
  • Information by UniProt

Recombinant Human Carbonic Anhydrase I protein images

  • 15% SDS-PAGE showing ab89359 at approximately 31kDa (3µg).
  • Anti-Carbonic Anhydrase I antibody (ab92649) at 1/500 dilution + Recombinant Human Carbonic Anhydrase I protein (ab89359) at 0.01 µg

    Secondary
    Goat Anti-Rabbit IgG H&L (HRP) preadsorbed (ab97080) at 1/5000 dilution
    Developed using the ECL technique

    Performed under reducing conditions.

    Exposure time : 20 seconds

References for Recombinant Human Carbonic Anhydrase I protein (ab89359)

ab89359 has not yet been referenced specifically in any publications.

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