Recombinant Human Glutathione S Transferase alpha 1 protein (ab95381)

Overview

Description

  • Nature
    Recombinant
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Species
      Human
    • Sequence
      MAEKPKLHYF NARGRMESTR WLLAAAGVEF EEKFIKSAED LDKLRNDGYL MFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYIEGIA DLGEMILLLP VCPPEEKDAK LALIKEKIKN RYFPAFEKVL KSHGQDYLVG NKLSRADIHL VELLYYVEEL DSSLISSFPL LKALKTRISN LPTVKKFLQP GSPRKPPMDE KSLEEARKIF RF

Specifications

Our Abpromise guarantee covers the use of ab95381 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

    Western blot

  • Purity
    > 90 % SDS-PAGE.
    purified by using conventional chromatography techniques
  • Form
    Liquid
  • 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
    • Glutathione S alkyltransferase A1
    • Glutathione S aryltransferase A1
    • Glutathione S transferase 2
    • Glutathione S transferase A1
    • Glutathione S transferase alpha 1
    • Glutathione S transferase Ha subunit 1
    • Glutathione S-transferase A1
    • GST class-alpha member 1
    • GST epsilon
    • GST HA subunit 1
    • GST, class alpha, 1
    • GST-epsilon
    • GST2
    • GSTA1
    • GSTA1 1
    • GSTA1-1
    • GSTA1_HUMAN
    • GTH1
    • HA subunit 1
    • MGC131939
    • OTTHUMP00000016611
    • S (hydroxyalkyl)glutathione lyase A1
    see all
  • Function
    Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
  • Tissue specificity
    Liver.
  • Sequence similarities
    Belongs to the GST superfamily. Alpha family.
    Contains 1 GST C-terminal domain.
    Contains 1 GST N-terminal domain.
  • Domain
    The C-terminal domain may form a component of the hydrophobic substrate-binding site, but in contrast appears not to be directly involved in GSH binding and is not absolutely essential for catalytic activity.
  • Cellular localization
    Cytoplasm.
  • Information by UniProt

Images

  • 15% SDS-PAGE image (3ug) generated using ab95381

References

ab95381 has not yet been referenced specifically in any publications.

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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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