Description

  • Product name

    Recombinant Human TRIM5 delta protein (His tag)
  • Purity

    > 95 % SDS-PAGE.
    The purity of ab196078 is greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.
  • Endotoxin level

    < 1.000 Eu/µg
  • Expression system

    HEK 293 cells
  • Accession

  • Protein length

    Protein fragment
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Sequence

      MGSSHHHHHHSSGLVPRGSHMASGILVNVKEEVTCPICLELLTQPLSLDC GHSFCQACLTANHKKSMLDKGESSCPVCRISYQPENIRPNRHVANIVEKL REVKLSPEGQKVDHCARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFL TEEVAREYQVKLQAALEMLRQKQQEAEELEADIREEKASWKTQIQYDKTN VLADFEQLRDILDWEESNELQNLEKEEEDILKSLTNSETEMVQQTQSLRE LISDLEHRLQGSVMELLQ
    • Predicted molecular weight

      31 kDa including tags
    • Amino acids

      1 to 248
    • Tags

      His tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab196078 in the following tested applications.

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

  • Applications

    HPLC

    SDS-PAGE

  • Form

    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on Dry Ice. Store at -80°C.

    pH: 7.4
    Constituents: 99% Phosphate Buffer, 0.87% Sodium chloride

    0.2 µM filtered solution.

General Info

  • Alternative names

    • EG667823
    • Gm8833
    • RING finger protein 88
    • RNF88
    • TRIM5
    • TRIM5_HUMAN
    • Tripartite motif containing 5 transcript variant iota
    • Tripartite motif containing 5 transcript variant kappa
    • Tripartite motif containing protein 5
    • Tripartite motif protein TRIM5
    • Tripartite motif-containing protein 5
    see all
  • Function

    Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Restricts infection by N-tropic murine leukemia virus (N-MLV) and equine infectious anemia virus (EIAV).
  • Pathway

    Protein modification; protein ubiquitination.
  • Sequence similarities

    Belongs to the TRIM/RBCC family.
    Contains 1 B box-type zinc finger.
    Contains 1 B30.2/SPRY domain.
    Contains 1 RING-type zinc finger.
  • Domain

    The B box-type zinc finger domain and the coiled-coil domain contribute to the higher and low order multimerization respectively which is essential for restriction activity (PubMed:22482711).
    The B30.2/SPRY domain acts as a capsid recognition domain. Polymorphisms in this domain explain the observed species-specific differences among orthologs (PubMed:22482711).
    The RING-type zinc finger domain confers E3 ubiquitin ligase activity and is essential for retrovirus restriction activity, autoubiquitination and higher-order multimerization (PubMed:22482711).
  • Post-translational
    modifications

    Degraded in a proteasome-independent fashion in the absence of viral infection but in a proteasome-dependent fashion following exposure to restriction sensitive virus.
    Autoubiquitinated in a RING finger- and UBE2D2-dependent manner. Monoubiquitinated by TRIM21. Deubiquitinated by Yersinia YopJ. Ubiquitination may not lead to proteasomal degradation.
  • Cellular localization

    Cytoplasm > P-body. Closely associates with proteasomal subunits in cytoplasmic bodies (By similarity). Colocalizes with SQSTM1 in cytoplasmic bodies.
  • Information by UniProt

References

ab196078 has not yet been referenced specifically in any publications.

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