Overview

Description

  • Nature
    Recombinant
  • Source
    Wheat germ
  • Amino Acid Sequence
    • Species
      Human
    • Sequence
      DNVGNLHFLYSELCKGAFHYGLTKDRKRRSQDGCPDGCASLTATAPSPEV SAAATISLMTDEPGLDNPAYVSSAEDGQPAISPVDSGRSNRTRARPFERS
    • Amino acids
      19 to 118
    • Tags
      proprietary tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab164648 in the following tested applications.

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

  • Applications

    Western blot

    ELISA

  • Form
    Liquid
  • Additional notes
    Protein concentration is above or equal to 0.05 mg/ml.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 8.00
    Constituents: 0.31% Glutathione, 0.79% Tris HCl

General Info

  • Alternative names
    • E3 ubiquitin protein ligase LNX
    • Ligand of Numb protein X 1
    • Ligand of numb protein X 1 E3 ubiquitin protein ligase
    • LNX
    • LNX1
    • MPDZ
    • Multi PDZ domain containing protein E3 ubiquitin protein ligase LNX
    • Numb binding protein 1
    • PDZ domain-containing ring finger protein 2
    • PDZRN2
    see all
  • Relevance
    Lnx1 is a membrane-bound protein that is involved in signal transduction and protein interactions. Lnx1 is an E3 Ubiquitin ligase protein that mediates ubiquitination and subsequent proteasomal degradation of proteins containing phosphotyrosine binding (PTB) domains. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Lnx1 mediates ubiquitination of isoform p66 and isoform p72 of NUMB, but not that of isoform p71 or isoform p65.
  • Cellular localization
    Cytoplasmic

Images

  • ab164648 on a 12.5% SDS-PAGE stained with Coomassie Blue.

References

ab164648 has not yet been referenced specifically in any publications.

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