Mouse VEGF188
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| Cat-Nr. | M30-094S |
| Size | 2 µg |
| Price | 80 € |
| Source | E. coli |
| Formulation | lyophilized |
| Purity Confirmation | > 95% by SDS-PAGE & silver stain |
| Length [aa] | 188 |
| Molecular Weight | 44.2 kDa |
| N Terminal Sequence | APTTEGE |
| Endotoxin Levels | < 0.1 ng per µg of mouse VEGF188 |
| Biological Activity | Measured by cell proliferation of human umbilical vein endothelial cells (HUVEC) in the range of 2-20 ng/ml. |
| Species Reactivity | Mouse |
| Buffer | 50 mM acetic acid |
| Reconstitution | The lyophilized VEGF188 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 VEGF188 should be stored in working aliquots at -20°C. |
| Synonyms | vascular endothelial growth factor A; Vegfa; Vpf; Vegf; Vegf188 |
| Description | Mouse Vascular Endothelial Growth Factor188 (VEGF188), a 22,1 kDa protein consisting of 188 amino acid residues, is produced as a homodimer. VEGF188 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 VEGF188 have been identified, VEGFR-1 (FLT-1), and VEGFR-2 (Flk-1). Consistent with the endothelial cell-specific action of VEGF188, 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 is also a chemo attractant for monocytes and endothelial cells. At least four different proteins are generated by differential splicing of the mouse VEGF gene: VEGF120, VEGF144, VEGF164 and VEGF188. The most abundant form is VEGF164. Whereas VEGF120 VEGF144, and VEGF164 are secreted proteins, VEGF188 is strongly cell-associated. In addition, the isoforms VEGF164 and VEGF188 bind to heparin with high affinity. VEGF is apparently a homodimer, but preparations of VEGF show some heterogeneity on SDS gels depending of the secretion of different forms and the varying degrees of glycosylation. All dimeric forms possess similar biological activities. There is evidence that heterodimeric molecules between the different isoforms exists and that different cells and tissues express different VEGF isoforms. A related protein of VEGF is placenta growth factor (PlGF) with about 53% homology and VEGF-B with similar biological activities. |
| Protein Sequence | APTTEGEQKSHEVIKFMDVYQRSYCRPIETLVDIFQEYPDEIEYIFKPSCVPLMRCAGCCNDEALECVPTSESNITMQIMRIKPHQSQHIGEMSFLQHSRCECRPKKDRTKPEKKSVRGKGKGQKRKRKKSRFKSWSVHCEPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR |
| Uniprot ID | Q00731 |
| Protein RefSeq | NP_001020421 |
| mRNA RefSeq | NM_001025250 |
Figures
SDS-PAGE analysis of recombinant mouse VEGF-A isoforms produced in E. coli. Samples were loaded under non-reducing conditions in 15% SDS-polyacrylamide gel and visualized with Silver staining.
Stimulation of cell proliferation in primary human umbilical vein endothelial cells (HUVEC) by recombinant moues VEGF-A isoforms. Values are the means (±SD) of triplicate determinations and expressed as percentage of control.
Reference
- Aerocyte specification and lung adaptation to breathing is dependent on alternative splicing changes. M. F. Fidalgo et al., Life Sci Alliance. 2022 Dec; 5(12): e202201554.
- VEGF188 promotes corneal reinnervation after injury. J. T. Brash et al., JCI Insight. 2019 Nov 1;4(21). pii: 130979.
- VEGF189 binds NRP1 and is sufficient for VEGF/NRP1-dependent neuronal patterning in the developing brain. M. Tillo et al., Development. 2015 Jan 15; 142(2): 314–319.
- Tumour Cells Expressing Single VEGF Isoforms Display Distinct Growth, Survival and Migration Characteristics. C. Kanthou et al., PLoS One. 2014; 9(8): e104015.
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