Overview

Description

  • Nature
    Recombinant
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species
      Human
    • Sequence
      MGSSHHHHHH SSGLVPRGSH MDGTFLWKIT NVTRRCHESA CGRTVSLFSP AFYTAKYGYK LCLRLYLNGD GTGKRTHLSL FIVIMRGEYD ALLPWPFRNK VTFMLLDQNN REHAIDAFRP DLSSASFQRP QSETNVASGC PLFFPLSKLQ SPKHAYVKDD TMFLKCIVET ST
    • Molecular weight
      20 kDa including tags
    • Amino acids
      266 to 416
    • Tags
      His tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab95858 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.
    ab95858 is purified 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: 20% Glycerol, 0.1M Sodium chloride, 20mM Tris HCl, 1mM DTT, pH 8.0

General Info

  • Alternative names
    • 4732496E14Rik
    • EBI6
    • EBV induced protein 6
    • Epstein-Barr virus-induced protein 6
    • MGC:10353
    • Tnf receptor associated factor 1
    • TNF receptor-associated factor 1
    • TRAF 1
    • TRAF1
    • TRAF1_HUMAN
    see all
  • Function
    Adapter molecule that regulates the activation of NF-kappa-B and JNK. Plays a role in the regulation of cell survival and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2.
  • Sequence similarities
    Contains 1 MATH domain.
  • Domain
    The coiled coil domain mediates homo- and hetero-oligomerization.
    The MATH/TRAF domain binds to receptor cytoplasmic domains.
    Cleavage by CASP8 liberates a C-terminal fragment that promotes apoptosis and inhibits the activation of NF-kappa-B in response to TNF signaling.
  • Post-translational
    modifications
    Polyubiquitinated by BIRC2 and/or BIRC3, leading to its subsequent proteasomal degradation.
  • Information by UniProt

Images

  • 15% SDS-PAGE showing ab95858 at approximately 19.5kDa (3µg).

References

ab95858 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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