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 0.1‑0.3 µg/mL. Measured by its binding ability in a functional ELISA. Immobilized recombinant human Flt-4 Fc Chimera at 5 µg/mL (100 µL/well) binds Recombinant Human VEGF‑D with an apparent KD <15 nM.
Source
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human VEGF-D protein Phe93-Ser201, with an N-terminal Met and C-terminal 6-His tag
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Bioactivity
Theoretical MW
13 kDa (monomer). 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
10-20 kDa, reducing conditions
Publications
Read Publications using 622-VD in the following applications:
Vascular endothelial 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 cystine 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 the 354 aa 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 - 6). Mature human VEGF-D shares 94%, 95%, 99%, 97% and 93% aa identity with mouse, rat, equine, canine and bovine VEGF-D, respectively (4, 5). 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 (7). Processed human VEGF-D is also a ligand for VEGF R2, also called Flk-1 or KDR (7). 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 (8‑10). Both promote tumor lymphangiogenesis (11). 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 (12, 13).
Roy, H. et al. (2006) FEBS Lett. 580:2879.
Otrock, Z.H. et al. (2007) Blood Cells Mol. Dis. 38:258.
Yamada, Y. et al. (1997) Genomics 42:483.
Stacker, S.A. et al. (1999) J. Biol. Chem. 274:32127.
McColl, B.K. et al. (2003) J. Exp. Med. 198:863.
McColl, B.K. et al. (2007) FASEB J. 21:1088.
Baldwin, M.E. et al. (2001) J. Biol. Chem. 276:19166.
Baldwin, M.E. et al. (2005) Mol. Cell. Biol. 25:2441.
Karpanen, T. et al. (2006) Am. J. Pathol. 169:708.
Orlandini, M. et al. (2006) J. Biol. Chem. 281:17961.
Stacker, S.A. et al. (2001) Nature Med. 7:186.
Karpanen, T. et al. (2006) FASEB J. 20:1462.
Vlahakis, N.E. et al. (2005) J. Biol. Chem. 280:4544.
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