Description

  • Product name

    Recombinant Human l Afadin protein
  • Purity

    > 95 % SDS-PAGE.

  • Expression system

    Escherichia coli
  • Protein length

    Protein fragment
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Amino acids

      1 to 141

Specifications

Our Abpromise guarantee covers the use of ab91389 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

  • Form

    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid repeated freeze / thaw cycles.

    pH: 7.50
    Constituents: 0.595% HEPES, 0.0292% EDTA, 50% Glycerol, 0.29% Sodium chloride

General Info

  • Alternative names

    • AF6
    • AFAD_HUMAN
    • Afadin
    • ALL1-fused gene from chromosome 6 protein
    • Mllt4
    • Protein Af-6
    • Protein AF6
    see all
  • Function

    Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton.
  • Involvement in disease

    Note=A chromosomal aberration involving MLLT4 is associated with acute leukemias. Translocation t(6;11)(q27;q23) with MLL/HRX. The result is a rogue activator protein.
  • Sequence similarities

    Contains 1 dilute domain.
    Contains 1 FHA domain.
    Contains 1 PDZ (DHR) domain.
    Contains 2 Ras-associating domains.
  • Domain

    The PDZ/DHR domain interacts with the C-terminus of nectin and the Pro-rich N-terminus domain interacts with F-actin.
  • Cellular localization

    Cell junction > adherens junction. Not found at cell-matrix AJs.
  • Information by UniProt

References

ab91389 has not yet been referenced specifically in any publications.

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