Overview

Description

  • Nature

    Recombinant
  • Source

    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species

      Escherichia coli
    • Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMDQFECI NVADAHQKLQ EKEAVLVDIR DPQSFAMGHA VQAFHLTNDT LGAFMRDNDF DTPVMVMCYH GNSSKGAAQY LLQQGYDVVY SIDGGFEAWQ RQFPAEVAYG A
    • Molecular weight

      15 kDa including tags
    • Amino acids

      1 to 108
    • Tags

      His tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab156746 in the following tested applications.

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

  • Applications

    Mass Spectrometry

    SDS-PAGE

  • Mass spectrometry

    MALDI-TOF
  • Purity

    > 95 % SDS-PAGE.
    ab156746 was purified using conventional chromatography techniques.
  • Form

    Liquid
  • 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

General Info

  • Alternative names

    • GlpE
    • RDS
    • Rhodanese
    • Thiosulfate sulfurtransferase
    • Thiosulfate sulfurtransferase GlpE
    • THTR_HUMAN
    • TST
    see all
  • Function

    Formation of iron-sulfur complexes, cyanide detoxification or modification of sulfur-containing enzymes. Other thiol compounds, besides cyanide, can act as sulfur ion acceptors. Also has weak mercaptopyruvate sulfurtransferase (MST) activity.
  • Sequence similarities

    Contains 2 rhodanese domains.
  • Domain

    The structure consists of 2 domains of very similar conformation, suggesting a common evolutionary origin. However, the sequences of the 2 domains are very different.
  • Cellular localization

    Mitochondrion matrix.
  • Information by UniProt

Images

  • 15% SDS-PAGE analysis of 3µg ab156746.

References

ab156746 has not yet been referenced specifically in any publications.

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