Rat VEGF-C152S
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| Cat-Nr. | R20-016 |
| Size | 5 µg |
| Price | 99 € |
| Source | Insect cells |
| Label | His-Tag |
| Formulation | lyophilized |
| Purity Confirmation | > 90% by SDS-PAGE |
| Length [aa] | 127 |
| Molecular Weight | 18.0 - 24.0 kDa |
| Biological Activity | (A) The proliferative response to rrVEGF-CC152S was assayed in VEGFR3-expressing porcine aortic endothelial (PAE) cells (in vitro). (B) The lymphangiogenic response to rrVEGF-CC152S loaded in a biopolymeric albumin-alginate microcapsules for targeted slow-release was assayed in male Wistar rats. |
| Species Reactivity | Rat |
| Buffer | 50 mM acetic acid |
| Stabilizer/Carrier | BSA (50-fold) |
| Reconstitution | The lyophilized VEGF-C152S is soluble in water and most aqueous buffers. The lyophilized VEGF-C152S should be reconstituted in PBS or medium to a concentration not lower than 50µg/ml. |
| Stability and Storage | Lyophilized samples are stable for greater than six months at -20°C to -70°C. Reconstituted VEGF-C152S should be stored in working aliquots at -20°C. Avoid repeated freeze-thaw cycles! |
| Synonyms | vascular endothelial growth factor C; Vegfc |
| Description | VEGF-C152S is a point mutant generated by the replacement of the second conserved Cys residue of the recombinant processed VEGF-C by a Ser residue. VEGF-C152S is analog to the human VEGF-C156S mutant and only active toward VEGFR-3/FLT-4 but, unlike wild type VEGF-C, is unable to bind to and to activate signalling through VEGFR-2/KDR. VEGF-C152S was inactive in the vascular permeability assay and did not increase migration of the capillary endothelial cells, indicating that these VEGF-like effects of VEGF-C require VEGFR-2 binding. VEGF-C, also known as Vascular Endothelial Growth Factor Related Protein (VRP), is a recently discovered VEGF growth factor family member that is most closely related to VEGF-D. The rat VEGF-C cDNA encodes a pre-pro-protein of 416 amino acids residues. It is almost identical to the mouse VEGF-C protein. Similar to VEGF-D, VEGF-C has a VEGF homology domain spanning the middle third of the precursor molecule and long N- and C-terminal extensions. In adults, VEGF-C is highly expressed in heart, placenta, ovary and small intestine. Recombinant rat VEGF-C, lacking the N- and C-terminal extensions and containing only the middle VEGF homology domain, forms primarily non-covalently linked dimers. This protein is a ligand for both VEGFR-2/KDR and VEGFR-3/FLT-4. Since VEGFR-3 is strongly expressed in lymphatic endothelial cells, it has been postulated that VEGF-C is involved in the regulation of the growth and/or differentiation of lymphatic endothelium. Although recombinant rat VEGF-C is also a mitogen for vascular endothelial cells, it is much less potent than VEGF-A. The recombinant rat VEGF-C contains 127 amino acids residues and was fused to a His-tag (6x His) at the C-terminal end. As a result of glycosylation VEGF-C migrates as an 18-24 kDa protein in SDS-PAGE under reducing conditions. |
| Protein Sequence | DTVKLAAAHYNTEILKSIDNEWRKTQCMPREVCIDVGKEFGAATNTFFKPPSVSVYRCGGCCNSEGLQCMNTSTGYLSKTLFEITVPLSQGPKPVTISFANHTSCRCMSKLDVYRQVHSIIHHHHHH |
| Uniprot ID | O35757 |
| Protein RefSeq | NP_446105.1 |
| mRNA RefSeq | NM_053653.1 |
Figures
SDS-PAGE analysis of recombinant rat VEGF-C152 mutant. Sample was loaded in 15% SDS-polyacrylamide gel under reducing conditions and stained with Coomassie blue.
In vivo: The lymphangiogenic response to recombinant rat VEGF-CC152S loaded in our biopolymeric albumin-alginate microcapsules for targeted slow-release was assayed in male Wistar rats. Briefly, after ischemia-reperfusion injury to induce myocardial infarction, VEGF-CC152S at the dose of 1.5 or 5 µg per heart was injected intra-myocardially. Lymphatic responses in the myocardium were analyzed by IHC at 3 weeks post-MI using LYVE1 antibody (RT, #103-PA50). Results are expressed as lymphatic vessel to cardiomyocyte ratio (mean ± sem).
The experiments were performed by the research group of Prof. Dr. E. Brakenhielm – Rouen University (see also: O. Henri et al., Circulation, March 2016, DOI: 10.1161)
In vitro: The proliferative response to recombinant rat VEGF-CC152S was assayed in VEGFR3-expressing porcine aortic endothelial (PAE) cells. Briefly, cells were plated in 12-well plates and incubated in DMEM medium supplemented with 1% fetal calf serum for cell cycle arrest 24h prior to stimulation of cell proliferation with recombinant VEGF-CC152S at the concentrations of 50 and 100 ng/mL. After 48h in culture, the cell proliferative response was assayed (WST-1 colorimetric assay), and the results expressed as % of control non-stimulated cells (mean ± sem).
The experiments were performed by the research group of Prof. Dr. E. Brakenhielm – Rouen University (see also: O. Henri et al., Circulation, March 2016, DOI: 10.1161)
Reference
- Biology of Vascular Endothelial Growth Factor C in the Morphogenesis of Lymphatic Vessels. K. Rauniyar et al., Front Bioeng Biotechnol. 2018; 6: 7.
- Selective Stimulation of Cardiac Lymphangiogenesis Reduces Myocardial Edema and Fibrosis Leading to Improved Cardiac Function Following Myocardial Infarction. O. Henri et al., Circulation. 2016 Apr 12;133(15):1484-97.
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