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Overview

  • Product nameVEGFC protein (His tag)See all VEGFC proteins and peptides ...
  • Protein descriptionRecombinant fusion protein (Rat) contains 129 amino acids residues, only the middle VEGF homology domain, was fused to a His-tag (6x His) at the C-terminal end.
  • Expression hostInsect cells

    • Properties

  • Purity> 90 % by SDS-PAGE
  • Purification notesPurity >90% by SDS-PAGE and visualised by silver stain. Product is a point mutant generated by the replacement of the second conserved Cys residue of the recombinant processed VEGFC by a Ser residue.
  • Biological activityThis product is analog to the human VEGF-C156S mutant and only active toward VEGFR-3/FLT -4 but, unlike wild type VEGF-C, is unable to bind to and to activate signalling through VEGFR-2/KDR.
  • FormLyophilised:Reconstitution: The lyophilised VEGFC is soluble in water and most aqueous buffers. The lyophilised VEGFC should be reconstituted in PBS or medium to a concentration not lower than 50 µg/ml.
  • Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
  • Storage bufferPreservative: None
    Constituents: PBS, BSA
  • Concentration information loading...
  • Additional notesSource: Insect cells.
  • Research Areas

    • Applications

    Our Abpromise guarantee covers the use of ab52146 in the following tested applications.

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

    Application Notes
    SDS-PAGE
  • Application notesSDS-PAGE: Use at an assay dependent dilution.
    As a result of glycosylation VEGFC migrates as an 18-24 kDa protein in
    SDS-PAGE under reducing conditions.

    Biological Activity: Measured by its ability to stimulate phosphorylation of the VEGFR-3/FLT-4 receptor in porcine aortic endothelial cells (PAE/FLT -4 cells). The ED50 for this effect is typically 150-300 ng/ml.
    Inactive in the vascular permeability assay.

    Not yet tested in other applications.
    Optimal dilutions/concentrations should be determined by the end user.

    • Protein info

    • Alternative names
        Flt 4LFlt4 ligandFLT4 ligand DHM
        Flt4-LFlt4LVascular endothelial growth factor CVascular endothelial growth factor related proteinVascular endothelial growth factor-related proteinVEGF CVEGF-CVegfcVEGFC_HUMANVRP
      see all
  • FunctionGrowth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates VEGFR-2 (KDR/FLK1) and VEGFR-3 (FLT4) receptors.
  • Tissue specificitySpleen, lymph node, thymus, appendix, bone marrow, heart, placenta, ovary, skeletal muscle, prostate, testis, colon and small intestine and fetal liver, lung and kidney, but not in peripheral blood lymphocyte.
  • Sequence similaritiesBelongs to the PDGF/VEGF growth factor family.
  • Post-translational
    modifications    Undergoes a complex proteolytic maturation which generates a variety of processed secreted forms with increased activity toward VEGFR-3, but only the fully processed form could activate VEGFR-2. VEGF-C first form an antiparallel homodimer linked by disulfide bonds. Before secretion, a cleavage occurs between Arg-227 and Ser-228 producing an heterotetramer. The next extracellular step of the processing removes the N-terminal propeptide. Finally the mature VEGF-C is composed mostly of two VEGF homology domains (VHDs) bound by non-covalent interactions.
  • Cellular localizationSecreted.

    • Target information above from: UniProt accession P49767 The UniProt Consortium
    The Universal Protein Resource (UniProt) in 2010
    Nucleic Acids Res. 38:D142-D148 (2010) .

    Information by UniProt

    References for VEGFC protein (His tag) (ab52146)

    ab52146 has not yet been referenced specifically in any publications.

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