Recombinant Human Thioredoxin domain containing 9 protein (ab40606)

Overview

  • Product name
    Recombinant Human Thioredoxin domain containing 9 protein
  • Protein length
    Full length protein

Description

  • Nature
    Recombinant
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Species
      Human

Associated products

Specifications

Our Abpromise guarantee covers the use of ab40606 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

  • Purity
    > 95 % SDS-PAGE.

  • Form
    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.

    Preservative: 0.002% Sodium Azide
    Constituents: 0.1% Triton-X-100, 10mM Tris, pH 8.0

General Info

  • Alternative names
    • APACD
    • ATP binding protein associated with cell differentiation
    • ATP-binding protein associated with cell differentiation
    • ES cell related protein
    • PHLP3
    • Phosducin like protein 3
    • Protein 1 4
    • Protein 1-4
    • Thioredoxin domain containing 9
    • Thioredoxin domain containing protein 9
    • Thioredoxin domain-containing protein 9
    • TXND9_HUMAN
    • Txndc9
    • TXNDC9 protein
    see all
  • Function
    Significantly diminishes the chaperonin TCP1 complex ATPase activity, thus negatively impacts protein folding, including that of actin or tubulin.
  • Sequence similarities
    Contains 1 thioredoxin domain.
  • Information by UniProt

Recombinant Human Thioredoxin domain containing 9 protein images

  • Analysis of TXNDC9 (ab40606) Recombinant Protein (1µg). Using 4-20% SDS gradient gel. Coomassie blue stained gel. A band can be seen at about 27 kDa.

References for Recombinant Human Thioredoxin domain containing 9 protein (ab40606)

ab40606 has not yet been referenced specifically in any publications.

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