Human VEGF121
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| Cat-Nr. | 300-072 |
| Size | 20 µg |
| Price | 315 € |
| Source | E. coli |
| Formulation | lyophilized |
| Purity Confirmation | > 98% by SDS-PAGE |
| Length [aa] | 121 |
| Molecular Weight | 28.4 kDa |
| N Terminal Sequence | APMAEGG |
| Endotoxin Levels | < 0.1 ng per µg of VEGF121 |
| Biological Activity | Measured in a cell proliferation assay using primary HUVECs. The ED50 for this effect is typically 2 - 10ng/mL. |
| Species Reactivity | Human |
| Buffer | 50mM acetic acid |
| Reconstitution | The lyophilized VEGF121 should be reconstituted in 50 mM acetic acid 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 VEGF121 should be stored in working aliquots at -20°C. Avoid repeated freeze-thaw cycles! |
| Synonyms | Vascular Endothelial Growth Factor A; VEGFA; VPF; VEGF; MVCD1 |
| Description | Human Vascular Endothelial Growth Factor121 (VEGF121), a 18 kDa protein consisting of 121 amino acid residues is produced as a homodimer. VEGF is a polypeptide growth factor and a member of the platelet-derived growth factor family. It is a specific mitogen for vascular endothelial cells and a strong angiogenic factor in vivo. Two high-affinity tyrosine kinase receptors for VEGF121 have been identified, VEGFR-1 (FLT-1), and VEGFR-2 (KDR). Consistent with the endothelial cell-specific action of VEGF121, expression of both receptor genes has been found predominantly but not exclusively on endothelial cells. Expression of VEGFR-1 was also found on human monocytes, neutrophils (PMNs), bovine brain pericytes and villous and extravillous trophoblasts. In addition to its action as a mitogen it is a potent vascular permeability factor (VPF) in vivo, and a chemoattractant molecule for monocytes and endothelial cells. Five different proteins are generated by differential splicing: VEGF121, VEGF145, VEGF165, VEGF189 and VEGF206. The most abundant form is VEGF165. Whereas VEGF121 and VEGF165 are secreted proteins, VEGF145, VEGF189 and VEGF206 are strongly cell-associated. The isoforms VEGF145, VEGF165 and VEGF189 bind to heparin with high affinity. VEGF121 is apparently a homo-dimer, but preparations of VEGF show some heterogeneity on SDS gels depending on the secretion of different forms and the varying degrees of glycosylation. All dimeric forms posses’ similar biological activities but the bioavailability is very different. There is good evidence that heterodimeric molecules between the different isoforms exist and that different cells and tissues express different VEGF isoforms. The other members of this increasing growth factor family are VEGF-B, -C, -D, -E and PlGF. |
| Protein Sequence | APMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKCDKPRR |
| Uniprot ID | P15692 |
| Protein RefSeq | NP_001020537.2 |
| mRNA RefSeq | NM_001025366.2 |
Figures
SDS-PAGE analysis of recombinant human VEGF121. Sample was loaded in 15% SDS-polyacrylamide gel under non-reducing condition and stained with Coomassie blue.
VEGF121-induced proliferation of primary human dermal lymphatic endothelial cells (HDLEC). HDLECs were stimulated with increasing amounts of recombinant human VEGF121.
Reference
- Receptor protein tyrosine phosphatase beta/zeta is a functional binding partner for vascular endothelial growth factor. M. Koutsioumpa et al., Mol Cancer. 2015; 14(1): 19.
- Spatial regulation of VEGF receptor endocytosis in angiogenesis. M. Nakayama et al., Nat Cell Biol.2 13 Mar; 15(3): 249–260.
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