Overview

Description

  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • AccessionP50552
    • SpeciesHuman
    • SequenceMGSSHHHHHHSSGLVPRGSHMSETVICSSRATVMLYDDGNKRWLPAGTGP QAFSRVQIYHNPTANSFRVVGRKMQPDQQVVINCAIVRGVKYNQATPNFH QWRDARQVWGLNFGSKEDAAQFAAGMASALEALEGGGPPPPPALPTWSVP NGPSPEEVEQQKRQQPGPSEHIERRVSNAGGPPAPPAGGPPPPPGPPPPP GPPPPPGLPPSGVPAAAHGAGGGPPPAPPLPAAQGPGGGGAGAPGLAAAI AGAKLRKVSKQEEASGGPTAPKAESGRSGGGGLMEEMNAMLARRRKATQV GEKTPKDESANQEEPEARVPAQSESVRRPWEKNSTTLPRMKSSSSVTTSE TQPCTPSSSDYSD
    • Molecular weight38 kDa including tags
    • Amino acids1 to 343
    • TagsHis tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab125773 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

  • Purity> 85 % SDS-PAGE.
    ab125773 is purified by proprietary chromatographic techniques. Purity is greater than 85.0% as determined by SDS-PAGE.
  • FormLiquid
  • Additional notesFor long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at -20°C. Store under Desiccating conditions.

    pH: 8.00
    Constituents: 0.002% PMSF, 0.08% DTT, 0.32% Tris HCl, 10% Glycerol, 1.17% Sodium chloride

General Info

  • Alternative names
    • Vasodilator stimulated phosphoprotein
    • Vasodilator-stimulated phosphoprotein
    • vasp
    • VASP_HUMAN
  • FunctionEna/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation.
  • Tissue specificityHighly expressed in platelets.
  • Sequence similaritiesBelongs to the Ena/VASP family.
    Contains 1 WH1 domain.
  • DomainThe EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization.
    The WH1 domain mediates interaction with XIRP1.
  • Post-translational
    modifications
    Major substrate for cAMP-dependent (PKA) and cGMP-dependent protein kinase (PKG) in platelets. The preferred site for PKA is Ser-157, the preferred site for PKG, Ser-239. In ADP-activated platelets, phosphorylation by PKA or PKG on Ser-157 leads to fibrinogen receptor inhibition. Phosphorylation on Thr-278 requires prior phosphorylation on Ser-157 and Ser-239. In response to phorbol ester (PMA) stimulation, phosphorylated by PKC/PRKCA. In response to thrombin, phosphorylated by both PKC and ROCK1. Phosphorylation at Thr-278 by AMPK does not require prior phosphorylation at Ser-157 or Ser-239. Phosphorylation modulates F-actin binding, actin filament elongation and platelet activation. Carbon monoxide (CO) promotes phosphorylation at Ser-157, while nitric oxide (NO) promotes phosphorylation at Ser-157, but also at Ser-239. Response to NO and CO is blunted in platelets from diabetic patients, and VASP is not phosphorylated efficiently at Ser-157 and Ser-239.
  • Cellular localizationCytoplasm. Cytoplasm > cytoskeleton. Cell junction > focal adhesion. Cell projection > lamellipodium membrane. Cell projection > filopodium membrane. Targeted to stress fibers and focal adhesions through interaction with a number of proteins including MRL family members. Localizes to the plasma membrane in protruding lamellipodia and filopodial tips. Stimulation by thrombin or PMA, also translocates VASP to focal adhesions. Localized along the sides of actin filaments throughout the peripheral cytoplasm under basal conditions.
  • Information by UniProt

References for Recombinant Human VASP protein (ab125773)

ab125773 has not yet been referenced specifically in any publications.

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