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Rat VEGFC / VEGF-C Protein (aa 108-223, Fc Tag)

VEGFC

Catalog Number P80103-R01H
Organism Species Rat
Host Human Cells
Synonyms VEGFC
Molecular Weight The recombinant Rat VEGFC/Fc comprises 376 amino acids and has a predicted molecular mass of 41.5 kDa. The apparent molecular mass of the protein is approximately 44 and 34 kDa in SDS-PAGE under reducing conditions.
predicted N Glu
SDS-PAGE
Purity > (73+25.1) % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the rat VEGFC (O35757) (Ala108-Arg223) was expressed, fused with the Fc region of human IgG1 at the N-terminus.
Bio-activity 1. Immobilized mouse FLT4-His (P50584-M08H) at 10 μg/mL (100 μL/well) can bind rat Fc-VEGFC, The EC50 of rat Fc-VEGFC is 0.41-0.95 μg/mL.
2. Measured in a cell proliferation assay using human umbilical vein endothelial cells (HUVEC). The ED50 for this effect is 20-100ng/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.