Human VEGF145
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| Cat-Nr. | 300-033-E |
| Size | 5 µg |
| Price | 145 € |
| Source | E. coli |
| Formulation | lyophilized |
| Purity Confirmation | > 95% by SDS-PAGE |
| Length [aa] | 145 |
| Molecular Weight | 34 kDa |
| N Terminal Sequence | APMAEGG |
| Endotoxin Levels | < 0.1 ng per µg of human VEGF145 |
| Biological Activity | The ED50 for stimulation of cell proliferation in human umbilical vein endothelial cells by VEGF145 has been determined to be in the range of 5-10 ng/ml. |
| Species Reactivity | Human |
| Buffer | 50mM acetic acid |
| Reconstitution | The lyophilized VEGF145 should be reconstituted in water to a concentration not lower than 50 µg/ml. For long term storage we recommend to add at least 0.1% human or bovine serum albumin. |
| Stability and Storage | Lyophilized samples are stable for greater than six months at -20°C to -70°C. Reconstituted VEGF145 should be stored in working aliquots at -20°C. |
| Synonyms | vascular endothelial growth factor A; VEGFA; VPF; VEGF; MVCD1 |
| Description | A vascular endothelial growth factor (VEGF) mRNA species containing exons 1–6 and 8 of the VEGF gene was found to be expressed as a major VEGF mRNA form in several cell lines derived from carcinomas of the female reproductive system. This mRNA is predicted to encode a VEGF form of 145 amino acids (VEGF145). VEGF145 produced in insect cells is a homodimeric, 20.5 kDa protein belonging to the VEGF-A family. Recombinant VEGF145 induced the proliferation of vascular endothelial cells and promoted angiogenesis in vivo. VEGF145 was compared with previously characterized VEGF species with respect to interaction with heparinlike molecules, cellular distribution, VEGF receptor recognition, and extracellular matrix (ECM) binding ability. VEGF145 shares with VEGF165 the ability to bind to the KDR/flk-1 receptor of endothelial cells. It also binds to heparin with an affinity similar to that of VEGF165. However, VEGF145 does not bind to two additional endothelial cell surface receptors that are recognized by VEGF165 but not by VEGF121. VEGF145 is secreted from producing cells as are VEGF121 and VEGF165. However, VEGF121 and VEGF165 do not bind to the ECM produced by corneal endothelial cells, whereas VEGF145 binds efficiently to this ECM. Basic fibroblast growth factor (bFGF)-depleted ECM containing bound VEGF145 induces proliferation of endothelial cells, indicating that the bound VEGF145 is active. The mechanism by which VEGF145 binds to the ECM differs from that of bFGF. Digestion of the ECM by heparinase inhibited the binding of bFGF to the ECM and released prebound bFGF, whereas the binding of VEGF145 was not affected by heparinase digestion. It therefore seems that VEGF145 possesses a unique combination of biological properties distinct from those of previously characterized VEGF species. The other members of this increasing growth factor family are VEGF-B, -C, -D and -E. Another member is the Placenta growth factor PlGF. |
| Protein Sequence | APMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKKSVRG KGKGQKRKRKKSRYKSWSVCDKPRR |
| Uniprot ID | P15692 |
| Protein RefSeq | NP_001191313.1 |
| mRNA RefSeq | NM_001025366.2 |
Figures
SDS-PAGE analysis of recombinant human VEGF-A isoforms produced in E. coli. Samples were loaded under non-reducing conditions in 15% SDS-polyacrylamide gel and stained with Silver stain.
VEGF145-induced proliferation of primary human dermal lymphatic endothelial cells (HDLEC). HDLECs were stimulated with increasing amounts of human VEGF145.
Reference
- VEGF receptor 2/-3 heterodimers detected in situ by proximity ligation on angiogenic sprouts. I. Nilsson et al., EMBO J. 2010 Apr 21;29(8):1377-88.
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