VEGF Mouse
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Description
Vascular Endothelial Growth Factor Mouse Recombinant produced in E.Coli is a disulfide-linked homodimeric, double polypeptide chains containing 165 amino acids and having a molecular mass of 38.8kDa.
Product Specs
Recombinant Mouse Vascular Endothelial Growth Factor, produced in E. coli, is a homodimeric protein with a disulfide bond. Each polypeptide chain consists of 165 amino acids, resulting in a molecular mass of 38.8 kDa for the dimer.
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The protein solution underwent filtration through a 0.2µm filter before being lyophilized in a buffer solution consisting of PBS with a pH of 7.4. |
(a) Analysis by RP-HPLC (Reverse Phase High-Performance Liquid Chromatography).
(b) Analysis by SDS-PAGE (Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis).
The biological activity of the protein is assessed by measuring its ability to stimulate the proliferation of human umbilical vein endothelial cells (HUVEC) in a dose-dependent manner. This is determined using a concentration range starting from 5.0 ng/ml, which corresponds to a specific activity of 200,000IU/mg.
Product Science Overview
Vascular Endothelial Growth Factor (VEGF) is a signal protein that stimulates the formation of blood vessels. It plays a crucial role in both physiological and pathological angiogenesis. The mouse recombinant form of VEGF is often used in research to study its effects and mechanisms in various biological processes.
VEGF was first identified as a factor that increases vascular permeability and was initially termed “vascular permeability factor” (VPF). It is now known to be a potent mitogen for endothelial cells, promoting their proliferation, migration, and new blood vessel formation (angiogenesis).
VEGF exists in several isoforms due to alternative splicing of its mRNA. The most common isoforms in mice are VEGF120, VEGF164, and VEGF188, corresponding to the number of amino acids in each variant. VEGF164 is the murine counterpart to human VEGF165 and is the most studied isoform due to its potent angiogenic activity .
VEGF exerts its effects by binding to specific receptors on the surface of endothelial cells. The primary receptors are VEGFR-1 (Flt-1) and VEGFR-2 (Flk-1/KDR). Binding of VEGF to these receptors activates a cascade of downstream signaling pathways that lead to endothelial cell proliferation, migration, and new blood vessel formation .
- Angiogenesis: VEGF is a key regulator of angiogenesis, the process by which new blood vessels form from pre-existing vessels. This is crucial during embryonic development, wound healing, and the menstrual cycle.
- Vascular Permeability: VEGF increases the permeability of blood vessels, allowing for the passage of proteins and other molecules into tissues.
- Endothelial Cell Survival: VEGF promotes the survival of endothelial cells by inhibiting apoptosis (programmed cell death).
VEGF is implicated in various pathological conditions, including cancer, diabetic retinopathy, and age-related macular degeneration. Tumors often secrete high levels of VEGF to promote the formation of new blood vessels, which supply the tumor with nutrients and oxygen, facilitating its growth and metastasis .
Given its role in angiogenesis, VEGF is a target for therapeutic intervention in diseases characterized by excessive or insufficient blood vessel formation. Anti-VEGF therapies, such as monoclonal antibodies (e.g., bevacizumab), are used to treat cancers and eye diseases by inhibiting VEGF activity .
