Human VEGF189
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| Cat-Nr. | 300-094 |
| Size | 5 µg |
| Price | 135 € |
| Source | E. coli |
| Formulation | lyophilized |
| Purity Confirmation | > 98% by SDS-PAGE |
| Length [aa] | 189 |
| Molecular Weight | ~ 42.0 kDa |
| N Terminal Sequence | APMAEGG |
| Endotoxin Levels | < 0.1 ng per µg of human VEGF189 |
| Biological Activity | Measured by the stimulation of cell proliferation in human umbilical vein endothelial cells in the range of 2-20 ng/ml. |
| Species Reactivity | Human |
| Buffer | 50mM acetic acid |
| Reconstitution | The lyophilized VEGF189 is soluble in water and most aqueous buffers. The lyophilized VEGF189 should be reconstituted in PBS or medium containing at least 0.1% human or bovine serum albumin to a concentration not lower than 50µg/ml. |
| Stability and Storage | The lyophilized protein is stable for a few weeks at room temperature, but best stored at –20°C. Reconstituted VEGF189 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 Factor VEGF189, a 21 kDa protein consisting of 189 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 VEGF165 have been identified, VEGFR-1 (FLT-1), and VEGFR-2 (KDR). Consistent with the endothelial cell-specific action of VEGF165, 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. VEGF165 is also a chemoattractant molecule for monocytes and endothelial cells. 5 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. VEGF165 is apparently a homodimer, but preparations of VEGF165 show some heterogeneity on SDS gels, depending on the secretion of different glycosylation patterns. All dimeric forms have similar biological activities but their bioavailability is very different. There is good evidence that there also exist heterodimeric molecules between the different isoforms and that different cells and tissues express different VEGF isoforms. 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 | APMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKKSVRGKGKGQKRKRKKSRYKSWSVPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR |
| Uniprot ID | P15692 |
| Protein RefSeq | NP_001020537.2 |
| 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 visualized with Silver stain.
VEGF-A Sandwich-ELISA using VEGF189 as standard. Mouse anti-human VEGF-A (Cat# 101-M56) was used as capture antibody, Biotinylated mouse anti-human VEGF-A #339 was used for detection.
VEGF189-induced proliferation of primary human dermal lymphatic endothelial cells (HDLEC). HDLECs were stimulated with increasing amounts of recombinant human VEGF189.
Reference
- VEGF-A165 is the predominant VEGF-A isoform in platelets, while VEGF-A121 is abundant in serum and plasma from healthy individuals. M. Yamakuchi et al., PLoS One. 2023; 18(4): e0284131.
- Angiogenesis and Functional Vessel Formation Induced by Interstitial Flow and Vascular Endothelial Growth Factor Using a Microfluidic Chip. Liu Y. et al., Micromachines (Basel). 2022 Jan 29;13(2):225.
- Tumor-secreted anterior gradient-2 binds to VEGF and FGF2 and enhances their activities by promoting their homodimerization. H. Guo et al., Oncogene. 2017 Sep 7;36(36):5098-5109.
- 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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