Rice Grain
Greater than 95.0% as determined by SDS-PAGE.
Vascular Endothelial Growth Factor Human Recombinant produced in Oryza Sativa has a molecular mass of 19.2kDa. The VEGF is purified by proprietary chromatographic techniques.
Vascular endothelial growth factor (VEGF) is a crucial signaling molecule for blood vessel development. While its effects have been primarily studied on vascular endothelial cells, VEGF also influences other cell types such as monocytes/macrophages, neurons, cancer cells, and kidney epithelial cells. VEGF enhances vascular permeability, stimulates vasculogenesis and endothelial cell production, promotes cell migration, and inhibits apoptosis. In laboratory settings, VEGF has been observed to stimulate endothelial cell division and movement. Additionally, VEGF acts as a vasodilator, increasing microvascular permeability; hence, it was initially known as vascular permeability factor. VEGF is present in healthy cartilage; however, only osteoarthritic cartilage expresses its receptors, NP1, VEGFR1, and VEGFR2. Notably, the concentration of VEGF in the culture medium of osteoarthritic chondrocytes was over three times higher than in the medium of normal chondrocytes.
Recombinant Human Vascular Endothelial Growth Factor, produced in Oryza Sativa (rice), has a molecular weight of 19.2kDa. The purification of VEGF is achieved through proprietary chromatographic methods.
The purity is determined to be greater than 95.0% via SDS-PAGE analysis.
The biological activity is determined by assessing the dose-dependent stimulation of human umbilical vein endothelial cell (HUVEC) proliferation. This assessment uses a concentration range of 10ng/ml, which corresponds to a Specific Activity of 100,000IU/mg.
Rice Grain
Vascular Endothelial Growth Factor (VEGF) is a signal protein that plays a crucial role in angiogenesis, the formation of new blood vessels from pre-existing ones. It is a member of the platelet-derived growth factor family of cystine-knot growth factors . VEGF is essential for both physiological processes, such as embryonic development and wound healing, and pathological conditions, including cancer and cardiovascular diseases .
VEGF is a glycoprotein that exists in several isoforms, with VEGF-A being the most studied. It binds to specific tyrosine kinase receptors (VEGFR-1 and VEGFR-2) on the surface of endothelial cells, triggering a cascade of signaling pathways that promote endothelial cell proliferation, migration, and survival . VEGF also increases vascular permeability, which is critical for the delivery of nutrients and oxygen to tissues .
Recombinant VEGF can be produced using various expression systems, including bacterial, yeast, insect, and mammalian cells. The choice of expression system depends on the desired yield, activity, and post-translational modifications of the protein. Recently, plants have emerged as a promising platform for the production of recombinant proteins, including VEGF .
Plants offer several advantages for recombinant protein production, such as low cost, scalability, and the ability to perform complex post-translational modifications. The production of human recombinant VEGF in plants involves the insertion of the VEGF gene into the plant genome, followed by the expression and purification of the protein. This approach has been successfully used to produce bioactive VEGF with similar properties to its native counterpart .
Recombinant VEGF has numerous applications in both research and clinical settings. It is used to study angiogenesis and vascular biology, develop therapeutic strategies for diseases involving abnormal blood vessel growth, and create tissue-engineered constructs for regenerative medicine. Additionally, VEGF-based therapies are being explored for the treatment of ischemic heart disease, wound healing, and cancer .