VEGF (121 a.a.) Human
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Description
Vascular Endothelial Growth Factor-121 Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide double chain containing 2x121 amino acids and having a molecular mass of 28.4kDa. VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates.
Product Specs
Recombinant Human Vascular Endothelial Growth Factor-121, produced in E. coli, is a non-glycosylated polypeptide chain dimer. Each monomer contains 121 amino acids, resulting in a molecular weight of 28.4 kDa for the dimer. Compared to other VEGF isoforms that bind strongly to vascular heparin sulfates, VEGF121 exhibits higher circulatory freedom.
The protein solution (1 mg/ml) was lyophilized without any additives.
Purity exceeds 98.0% as determined by:
(a) Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) analysis.
(b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis.
Compared to established standards, VEGF-121 demonstrates full biological activity. Activity is measured by the dose-dependent proliferation of Human Umbilical Vein Endothelial Cells (HUVECs), typically falling within the range of 1-6 ng/ml. This corresponds to a specific activity of 166,667-1,000,000 U/mg.
Product Science Overview
Vascular Endothelial Growth Factor (VEGF) is a signal protein that stimulates the formation of blood vessels. It is a part of the PDGF/VEGF growth factor family and plays a crucial role in both vasculogenesis (the formation of the circulatory system) and angiogenesis (the growth of blood vessels from pre-existing vasculature). VEGF is particularly important in the context of cancer, where it can promote tumor growth by increasing blood supply to the tumor.
VEGF-A, the most studied member of the VEGF family, exists in several isoforms due to alternative splicing of its mRNA. These isoforms include VEGF121, VEGF165, VEGF189, and VEGF206, among others. Each isoform has distinct properties and roles in angiogenesis. VEGF121, the focus of this article, is one of the smaller isoforms and lacks certain heparin-binding domains present in other isoforms.
VEGF121 is a homodimeric glycoprotein consisting of two identical subunits linked by disulfide bonds. It has a molecular weight of approximately 37 kDa as a homodimer and 50 kDa as a homotrimer . The recombinant form of VEGF121 is often expressed in human HEK 293 cells, which allows for authentic glycosylation, contributing to its stability in cell growth media and other applications .
VEGF121 is a potent angiogenic factor and mitogen that stimulates the proliferation, migration, and formation of endothelial cells. It also increases the permeability of blood vessels. VEGF121 is secreted by many cell types, including endothelial cells, macrophages, and T cells . Its expression is induced by hypoxia, inflammatory cytokines, and oncogene products in tumors .
VEGF121 exerts its effects by binding to specific receptor tyrosine kinases on the surface of endothelial cells, primarily VEGFR1 and VEGFR2. This binding activates several downstream signaling pathways, including the PI3K/Akt, p38 MAPK, and FAK pathways . These pathways promote endothelial cell survival, proliferation, and migration, all of which are essential for angiogenesis.
VEGF121 plays a key role in tumor angiogenesis, making it a target for cancer therapy. Inhibitors of VEGF and its receptors are used to treat various cancers by blocking the blood supply to tumors. Additionally, VEGF121 is involved in other pathological conditions characterized by abnormal blood vessel growth, such as age-related macular degeneration and diabetic retinopathy.
Recombinant VEGF121 is widely used in research to study angiogenesis and related processes. It is also used in cell culture to promote the growth and maintenance of endothelial cells. The recombinant protein is typically supplied as a lyophilized powder and can be reconstituted in aqueous solutions for use in various assays .
