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CYT-284

重組大鼠血管內(nèi)皮生長(zhǎng)因子相關(guān)蛋白（rrVEGF-C152）

2μg/10μg/1mg

Prospec

Background:
	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-C 152S is analog to the human VEGF-C 156S 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.
	Description :
	recombinant rat VEGF-C 152 contains 152 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.
	Physical Appearance:
	Sterile Filtered White lyophilized （freeze-dried） powder.
	Formulation:
	The protein was lyophilized from a concentrated （1mg/ml） solution with BSA.
	Solubility:
	It is recommended to reconstitute the lyophilized Recombinant Rat VEGF-C 152 in sterile 18MΩ-cm H₂O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
	Stability:
	Lyophilized Rat VEGF-C152 although stable at room temperature for 3 weeks, should be stored desiccated below -18⁰C. Upon reconstitution VEGF-C 152 should be stored at 4⁰C between 2-7 days and for future use below -18⁰C. Please prevent freeze-thaw cycles.
	Purity:
	Greater than 90.0% as determined by: （a） Analysis by RP-HPLC. （b） Anion-exchange FPLC. （c） Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.
	Dimers and aggregates:
	Less than 1% as determined by silver-stained SDS-PAGE gel analysis.
	Biological Activity:
	Measured by its ability to stimulate phosphorylation of the VEGFR-3/FLT-4 receptor in porcine aortic endothelial cells （PAE/FLT -4 cells）. The ED50 for this effect is typically 150-300 ng/ml, corresponding to a specific activity of 5 x 10³ Units/mg.
	Endotoxin:
	Less than 0.1 ng/µg （IEU/µg） of Rat VEGF-C152.
	Protein content:
	Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm. 2. Analysis by RP-HPLC, using a calibrated solution of VEGF-C152 as a Reference Standard.
	Usage:
	Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Latest Publications:

1. Molecular mechanisms of VEGF-A action during tissue repair.

J Investig Dermatol Symp Proc 2006 Sep;11（1）:79-86

2. Novel therapeutic developments other than EGFR and VEGF inhibition in colorectal cancer.

Oncologis t 2006 Oct;11（9）:1018-24

3. Heparin-II domain of fibronectin is a vascular endothelial growth factor-binding domain: enhancement of VEGF biological activity by a singular growth factor/matrix protein synergism.

Circ Res 2006 Oct 13;99（8）:853-60

4. Early vascular and neuronal changes in a VEGF transgenic mouse model of retinal neovascularization.

Invest Ophthalmol Vis Sci 2006 Oct;47（10）:4638-45

5. HDAC3 is crucial in shear- and VEGF-induced stem cell differentiation toward endothelial cells.

J Cell Biol 2006 Sep 25;174（7）:1059-69

6. Serum vascular endothelial growth factor （VEGF） and bcl-2 levels in advanced stage non-small cell lung cancer.

Cancer Invest 2006 Oct;24（6）:576-80

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