VEGF C Human
Greater than 90.0% as determined by SDS-PAGE.
Description
VEGF-C Human Recombinant- contains 121 amino acids residues including 6 amino acid His-tag fused at the C-terminal end. As a result of glycosylation VEGF-C migrates as an 18-24 kDa protein in SDS-PAGE under reducing conditions.
Product Specs
Recombinant Human VEGF-C encompasses 121 amino acid residues, including a C-terminally fused 6-amino acid His-tag. Glycosylation results in an observed molecular weight of 18-24 kDa for VEGF-C under reducing conditions in SDS-PAGE analysis.
Purity exceeds 90.0% as determined by SDS-PAGE analysis.
Biological activity is evaluated based on the capacity to stimulate VEGFR-3/FLT-4 receptor phosphorylation in PAEC/VEGFR3 cells and to induce proliferation in primary HDLEC cells.
Product Science Overview
Vascular Endothelial Growth Factor C (VEGF-C) is a member of the platelet-derived growth factor/vascular endothelial growth factor (PDGF/VEGF) family. It plays a crucial role in angiogenesis, lymphangiogenesis, and endothelial cell growth and survival. VEGF-C also affects the permeability of blood vessels .
VEGF-C is synthesized as a 58 kDa molecule consisting of a VEGF homology domain (VHD) flanked by N- and C-terminal propeptides . The VEGF family, including VEGF-C, does not share high homology but shares a cysteine knot motif comprising eight conserved cysteine residues . VEGF-C binds to VEGFR-3, mediating the activation of pathways required for lymphangiogenesis and angiogenesis .
VEGF-C is active in angiogenesis, the process of forming new blood vessels from existing vasculature, and lymphangiogenesis, the formation of lymphatic vessels . It promotes endothelial cell growth, survival, and migration, which are essential for tissue development, organ function, and wound healing . VEGF-C also increases vascular permeability, allowing for the exchange of nutrients and waste products between blood and tissues .
Recombinant human VEGF-C is produced using various expression systems, including Escherichia coli (E. coli) and mammalian cells . The recombinant protein is purified using techniques such as nickel affinity chromatography to obtain a high yield of active soluble protein . The biological activity of recombinant VEGF-C is tested using assays like the Chicken chorioallantoic membrane assay and wound-healing migration and proliferation assays on human umbilical vein endothelial cells (HUVEC) .
VEGF-C has potential therapeutic applications in treating diseases related to abnormal blood and lymphatic vessel formation, such as cancer, diabetic retinopathy, and age-related macular degeneration . Anti-VEGF therapies are commonly used in clinical practice to inhibit pathological angiogenesis and lymphangiogenesis . Understanding the mechanisms underlying VEGF-C’s role in these processes can help improve anti-angiogenesis and anti-lymphangiogenesis therapies .
