VEGF Rat (120a.a.), Yeast
Saccharomyces cerevisiae
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Sterile Filtered White lyophilized (freeze-dried) powder.
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Description
Vascular Endothelial Growth Factor(120a.a.) Rat Recombinant produced in yeast is a disulfide-linked homodimer consisting of 2x121 amino acid polypeptide chains, having a molecular mass of approximately 18.5kDa each.
VEGF is purified by proprietary chromatographic techniques.
Product Specs
Vascular endothelial growth factor (VEGF) is a key signaling protein that plays a vital role in angiogenesis (formation of new blood vessels) and vasculogenesis (development of the circulatory system). VEGF primarily affects vascular endothelial cells but also impacts other cell types, including monocytes/macrophages, neurons, cancer cells, and kidney epithelial cells. It contributes to increased vascular permeability, promotes angiogenesis and vasculogenesis, stimulates endothelial cell growth and migration, and inhibits apoptosis (programmed cell death). In vitro studies have demonstrated VEGF's ability to enhance endothelial cell division (mitogenesis) and migration. VEGF also acts as a vasodilator, widening blood vessels, and increases microvascular permeability, initially known as vascular permeability factor. Notably, elevated VEGF levels are associated with POEMS syndrome (Crow-Fukase syndrome). Moreover, mutations in the VEGF gene have been linked to both proliferative and nonproliferative diabetic retinopathy.
Recombinant Rat Vascular Endothelial Growth Factor (120a.a.), produced in yeast, is a homodimer protein consisting of two identical polypeptide chains, each comprising 121 amino acids. The two chains are linked together by disulfide bonds, resulting in a total molecular weight of approximately 18.5 kDa per chain. The purification process involves proprietary chromatographic techniques to ensure high purity.
Sterile Filtered White lyophilized (freeze-dried) powder.
The product is lyophilized (freeze-dried) from a concentrated solution in phosphate-buffered saline (PBS) at a pH of 7.4. The solution is sterile-filtered through a 0.2-micrometer filter before lyophilization.
To reconstitute the lyophilized Vascular Endothelial Growth Factor, it is recommended to dissolve it in sterile 18 megaohm-centimeter (MΩ·cm) H₂O (water) at a concentration of at least 100 micrograms per milliliter (µg/ml). The reconstituted solution can then be further diluted to desired concentrations in other aqueous solutions as needed.
Lyophilized VEGF, while stable at room temperature for up to 3 weeks, should ideally be stored in a dry environment (desiccated) at a temperature below -18°C for long-term storage. After reconstitution, Vascular Endothelial Growth Factor should be stored at 4°C and used within 2-7 days. For long-term storage of the reconstituted solution, it is recommended to store it below -18°C. Avoid repeated freeze-thaw cycles to maintain protein integrity and activity.
The purity of the Vascular Endothelial Growth Factor is greater than 90%, as determined by two analytical methods:
(a) Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC)
(b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE).
The biological activity of Vascular Endothelial Growth Factor is determined by its effective dose 50 (ED₅₀), which refers to the concentration required to achieve 50% of the maximum biological response. In this case, the ED₅₀ was measured using a cell proliferation assay with HUVEC (human umbilical vein endothelial cells) and was found to be in the range of 2-10 nanograms per milliliter (ng/ml).
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Saccharomyces cerevisiae
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Product Science Overview
Vascular Endothelial Growth Factor (VEGF) is a critical signaling protein involved in both angiogenesis (the formation of new blood vessels from pre-existing vessels) and vasculogenesis (the formation of entirely new blood vessels during embryonic development). VEGF plays a pivotal role in the body’s ability to supply oxygen and nutrients to tissues by promoting the growth of blood vessels. This protein is particularly important in conditions where tissues are deprived of oxygen, such as in wound healing and the growth of tumors.
The specific form of VEGF in question, Vascular Endothelial Growth Factor (120a.a.) (Rat Recombinant, Yeast), is a recombinant protein produced in yeast. It consists of 120 amino acids and is a disulfide-linked homodimer, meaning it is composed of two identical polypeptide chains linked by disulfide bonds. Each polypeptide chain has a molecular mass of approximately 18.5 kDa .
This recombinant form of VEGF is produced using the yeast expression system, specifically Saccharomyces cerevisiae. The yeast system is often used for the production of recombinant proteins due to its ability to perform post-translational modifications and its ease of scaling up for industrial production. The VEGF protein is purified using proprietary chromatographic techniques to ensure high purity and activity .
VEGF is known for its ability to stimulate endothelial cell mitogenesis (cell division) and cell migration. It also increases vascular permeability and acts as a vasodilator. These properties make VEGF a key player in the formation of new blood vessels. In vitro studies have shown that VEGF can stimulate the proliferation of human umbilical vein endothelial cells (HUVECs) at concentrations as low as 2-10 ng/ml .
Elevated levels of VEGF have been associated with various pathological conditions, including cancer, diabetic retinopathy, and POEMS syndrome (a rare blood disorder). In cancer, VEGF promotes tumor growth by ensuring an adequate blood supply to the rapidly dividing cancer cells. As a result, VEGF has become a target for anti-cancer therapies aimed at inhibiting its activity and thereby restricting the blood supply to tumors .
Recombinant VEGF proteins, such as the 120 amino acid form from rats, are used extensively in research to study angiogenesis and related processes. They are also used in the development of therapeutic agents aimed at modulating angiogenesis in various diseases. For example, VEGF inhibitors are used in the treatment of certain cancers and eye diseases like age-related macular degeneration.
