Reactivity | MuSpecies Glossary |
Applications | Binding Activity, Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured in a cell proliferation assay using HMVEC human microvascular endothelial cells. Marconcini, L. et al. (1999) Proc. Natl. Acad. Sci. USA 96:9671. The ED50 for this effect is 0.2‑0.8 µg/mL. Measured by its binding ability in a functional ELISA. Immobilized rmFlt-4/Fc Chimera at 5 µg/mL (100 µL/well) can bind rmVEGF-D with an apparent KD < 50 nM. |
Source | Spodoptera frugiperda, Sf 21 (baculovirus)-derived mouse VEGF-D protein Phe98-Ser206, with a C-terminal 6-His tag |
Accession # | |
N-terminal Sequence | Phe98 |
Protein/Peptide Type | Recombinant Proteins |
Gene | Figf |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
|
|
Theoretical MW | 13 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
|
SDS-PAGE | 14-20 kDa, reducing conditions |
|
Publications |
|
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
Vascular endothelia growth factor D (VEGF-D), also known as c-fos-induced growth factor (FIGF), is a secreted glycoprotein of the VEGF/PDGF family. VEGFs regulate angiogenesis and lymphangiogenesis during development and tumor growth, and are characterized by eight conserved cysteine residues that form a cysteine-knot structure (1 - 3). VEGF-C and VEGF-D, which share 23% amino acid (aa) sequence identity, are uniquely expressed as preproproteins that contain long N- and C-terminal propeptide extensions around the VEGF homology domain (VHD) (1, 2). Proteolytic processing of either 358 aa or 326 aa splice forms of mouse VEGF-D preproprotein creates a secreted proprotein. Further processing by extracellular serine proteases, such as plasmin or furin-like proprotein convertases, forms mature VEGF-D consisting of non-covalently linked 42 kDa homodimers of the 117 aa VHD (4 - 7). Mature mouse VEGF-D shares 94%, 99%, 93%, 91% and 89% aa identity with the VHD of human, rat, equine, canine and bovine VEGF-D, respectively. It is expressed in adult lung, heart, muscle, and small intestine, and is most abundantly expressed in fetal lungs and skin (1 - 4). Mouse and human VEGF-D are ligands for VEGF receptor 3 (VEGF-R3, also called Flt-4) that are active across species and show enhanced affinity when processed (8). Unlike human VEGF-D, which is also a ligand for VEGF-R2 (also called Flk-1 or KDR), mouse VEGF-D does not bind to VEGF-R2 (8). VEGF-R3 is strongly expressed in lymphatic endothelial cells and is essential for regulation of the growth and differentiation of lymphatic endothelium (1, 2). While VEGF-C is the critical ligand for VEGF-R3 during embryonic lymphatic development, VEGF-D is most active in neonatal lymphatic maturation and bone growth (9 - 11). Both promote tumor lymphangiogenesis (12). Consonant with their activity on VEGF receptors, binding of VEGF-C and VEGF-D to neuropilins contributes to VEGF-R3 signaling in lymphangiogenesis, while binding to integrin alpha 9 beta 1 mediates endothelial cell adhesion and migration (13, 14).
The concentration calculator allows you to quickly calculate the volume, mass or concentration of your vial. Simply enter your mass, volume, or concentration values for your reagent and the calculator will determine the rest.