Overview

Description

  • NatureSynthetic
  • Amino Acid Sequence
    • SpeciesHuman
    • SequencePQGPAFPEPGTATGS
    • Amino acids425 to 439

Associated products

Specifications

Our Abpromise guarantee covers the use of ab39756 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

    Blocking - Blocking peptide for Anti-DOK1 antibody (ab8112)

  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

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

    Preservative: 0.02% Sodium Azide
    Constituents: 0.01% BSA, PBS, pH 7.2

General Info

  • Alternative names
    • Docking protein 1
    • Docking protein 1 62kD
    • DOK 1
    • DOK1
    • DOK1_HUMAN
    • Downstream of tyrosine kinase 1
    • p62(dok)
    • P62DOK
    • pp62
    see all
  • FunctionDOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding site on ITGB3.
  • Tissue specificityExpressed in pancreas, heart, leukocyte and spleen. Expressed in both resting and activated peripheral blood T-cells.
  • Sequence similaritiesBelongs to the DOK family. Type A subfamily.
    Contains 1 IRS-type PTB domain.
    Contains 1 PH domain.
  • DomainThe PTB domain mediates receptor interaction.
  • Post-translational
    modifications
    Constitutively tyrosine-phosphorylated.
    Phosphorylated on tyrosine residues by the insulin receptor kinase. Results in the negative regulation of the insulin signaling pathway.
  • Cellular localizationCytoplasm and Cytoplasm > perinuclear region.
  • Information by UniProt

References for Human DOK1 peptide (ab39756)

ab39756 has not yet been referenced specifically in any publications.

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