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Human VEGF-C Protein (His Tag)

Flt4-L,LMPH1D,VEGF-C,VRP

Catalog Number P10542-H08H
Organism Species Human
Host Human Cells
Synonyms Flt4-L,LMPH1D,VEGF-C,VRP
Molecular Weight The recombinant mature form of human VEGFC consists of 136 amino acids and has a predicted molecular mass of 15.5 kDa. In SDS-PAGE under reducing conditions, it migrates with an apparent molecular mass of 22-24 kDa due to glycosylation.
predicted N Thr 103
SDS-PAGE
Purity > 97 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the mature form of human VEGFC (NP_005420.1) corresponding to amino acid (Thr 103-Arg 227) was expressed with a C-terminal polyhistidine tag.
Bio-activity 1. Measured by its binding ability in a functional ELISA .
Scatchard analysis showed the affinity constant (Kd) of recombinant human VEGF-C bound to recombinant human VEGFR3 was 1.4 nM .
2. Measured in a cell proliferation assay using human umbilical vein endothelial cells (HUVEC).
The ED50 for this effect is 0.1-0.5μg/mL.
Research Area Cancer |Signal transduction |Growth Factor & Receptor |Vascular Endothelial Growth Factor (VEGF) & Receptor |Vascular Endothelial Growth Factor (VEGF)
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Vascular endothelial growth factor C (VEGF-C) is a member of the VEGF family. Upon biosynthesis, VEGF-C protein is secreted as a non-covalent momodimer in an anti-parellel fashion. VEGF-C protein is a dimeric glycoprotein, as a ligand for two receptors, VEGFR-3 (Flt4), and VEGFR-2. VEGF-C may function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis. VEGF-C protein is over-expressed in various human cancers including breast cancer and prostate cancer. VEGF-C/VEGFR-3 axis, through different signaling pathways, plays a critical role in cancer progression by regulating different cellular functions, such as invasion, proliferation, and resistance to chemotherapy. Thus, targeting the VEGF-C/VEGFR-3 axis may be therapeutically significant for certain types of tumors.
Reference
  • Joukov V, et al. (1997) Vascular endothelial growth factors VEGF-B and VEGF-C. J Cell Physiol. 173(2): 211-5.
  • Su JL, et al. (2007) The role of the VEGF-C/VEGFR-3 axis in cancer progression. Br J Cancer. 96(4): 541-5.
  • Anisimov A, et al. (2009) Activated forms of VEGF-C and VEGF-D provide improved vascular function in skeletal muscle. Circ Res. 104(11): 1302-12.