Catalogue number
CYT-241
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Introduction
Vascular endothelial growth factor (VEGF) is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ). VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of the VEGF protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in the VEGF gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Description
Vascular Endothelial Growth Factor Human Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38.2kDa.
The VEGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
The VEGF protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Solubility
It is recommended to reconstitute the lyophilized VEGF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability
Lyophilized VEGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Amino acid sequence
APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENPCGPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR
Biological Activity
Determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 3.7-5.6 ng/ml, corresponding to a Specific Activity of 178,570-270,270IU/mg.
Protein content
VEGF protein quantitation was carried out by two independent methods:
1. UV spectroscopy at 280 nm using the absorbency value of 0.2875 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
2. Analysis by RP-HPLC, using a calibrated solution of VEGF 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.
Safety Data Sheet
References
1. Title:Expression of VEGF and Its Receptors in the Bovine Endometrium Throughout the Estrous Cycle: Effects of VEGF on Prostaglandin Production in Endometrial Cells.
Publication:Journal of Reproduction and Development
Vol. 56 (2010) No. 2 April P 223-229 \
Link:https://www.jstage.jst.go.jp/article/jrd/56/2/56_09-139S/_article
2.
Title: Cardio-specific long-term gene expression in a porcine model after
selective pressure-regulated retroinfusion of adeno-associated viral (AAV)
vectors
Publications: Gene
therapy
15.1 (2008): 12-17.
Link: http://www.nature.com/gt/journal/v15/n1/full/3303035a.html
3. Title: SU11248, A selective tyrosine kinases
inhibitor suppresses breast tumor angiogenesis and growth via targeting both
tumor vasculature and breast cancer cells
Publication: Cancer biology &
therapy 10.7 (2010): 703-711.
Link: http://www.tandfonline.com/doi/full/10.4161/cbt.10.7.12904
