Orf virus VEGF-E, Heparin-binding
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| Cat-Nr. | 300-046S |
| Size | 5 µg |
| Price | 140 € |
| Source | Insect cells |
| Formulation | lyophilized |
| Purity Confirmation | > 90% by SDS-PAGE |
| Length [aa] | 154 |
| Molecular Weight | 44 kDa (Dimer) |
| Biological Activity | Measured in a cell proliferation assay using primary HUVECs. The ED50 for this effect is typically 1 – 5 ng/mL. |
| Species Reactivity | Orf Virus |
| Buffer | 50 mM acetic acid |
| Reconstitution | The lyophilized ov-HB-VEGF-E should be reconstituted in 50 mM acetic acid to a concentration not lower than 50 µg/ml. For long term storage we would 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 HB-VEGF-E should be stored in working aliquots at -20°C. |
| Synonyms | Vascular Endothelial Growth Factor-E |
| Description | A DNA sequence encoding the first 116 amino acid residue of Orf virus VEGF-E isolate D1701 (Dehio et al., 1999 EMBO J. 18:363-374; GenBank accession No. AF106020) was fused with a DNA sequence encoding to the C-terminal heparin binding domain of human VEGF165. The chimeric protein was expressed in insect cells using a baculovirus expression system. Based on sequence similarity to VEGF-A, a gene encoding a VEGF homologue has recently been discovered in the genome of Orf virus (OV) (Lyttle et al., 1994 J. Virol 68:84-92). Different isolates of orf virus show significant amino acid sequence similarity to VEGF-A and described as a viral virulence factor that appear to be derived from captured host genes. All eight cysteine residues of the central cysteine knot motif characteristic of members of the VEGF family are conserved among other residues in the VEGF-E proteins (Dehio et al., 1999 EMBO J. 18:363-374; Wise et al., 1999 Proc. Natl. Acad. Sci USA 96:3071-3076). Alignment of all mammalian VEGF sequences indicated that VEGF-E is distinct from the previously described VEGFs but most closely related to VEGF-A. Like VEGF-A, VEGF-E was found to bind with high affinity to VEGF receptor-2 (KDR) resulting in receptor autophosphorylation, whilst in contrast to VEGF-A, VEGF-E and hb-VEGF-E can not bind to VEGF receptor-1 (Flt-1). Therefore VEGF-E is a potent angiogenic factor selectively binding to VEGF receptor–2/ KDR. Compared to human VEGF165 this virus form has no heparin-binding domain and seems to be a freely secreted protein comparable to VEGF121. In order to compare this form with human VEGF165, an additional heparin-binding domain was engineered at the C-terminus to allow interaction with proteo-aminoglycans and heparan sulfate. These form is also able to interact with neuropillin–1. |
| Protein Sequence | DSTKTWSEVFENSGCKPRPMVFRVHDEHPELTSQRFNPPCVTLMRCGGCCNDESLECVPTEEANVTMQLMGASVSGGNGMQHLSFVEHKKCDCKPPRDRARQENPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR |
| Uniprot ID | Q9YMF3 |
| Protein RefSeq | AAD03735.1 |
| mRNA RefSeq | AF106020.1 |
Figures
SDS-PAGE analysis of recombinant ov-HB-VEGF-E. Sample was loaded in 15% SDS-polyacrylamide gel under reducing conditions and stained with Coomassie blue.
Stimulation of cell proliferation in primary human umbilical vein endothelial cells (HUVEC) by recombinant ov-VEGF-E and ov-HB-VEGF-E. Values are the means (±SD) of triplicate determinations and expressed as percentage of control.
Reference
- Carbon monoxide inhibits sprouting angiogenesis and vascular endothelial growth factor receptor-2 phosphorylation. S. Ahmad et al., Thromb Haemost. 2015 Feb;113(2):329-37.
- Matrix-binding vascular endothelial growth factor (VEGF) isoforms guide granule cell migration in the cerebellum via VEGF receptor Flk1. C. Ruiz de Almodovar et al., J Neurosci. 2010 Nov 10;30(45):15052-66.
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