SajStorLab

Vascular Endothelial Growth Factor is one of the key regulators of angiogenesis. The most important role in the human body is played by a protein of the VEGF family called VEGF-A. VEGF-A is a 45 kDa glycoprotein homodimer and plays a key role in chemotaxis and angioblast differentiation, endotheliocyte (EC) proliferation, vasculogenesis, and vascular remodeling. As a result of alternative splicing or proteolytic cleavage, 4 main isoforms of VEGF-A are formed, consisting of 121, 165, 189, or 206 amino acid residues.

Vascular Endothelial Growth Factor is one of the key regulators of angiogenesis. The most important role in the human body is played by a protein of the VEGF family called VEGF-A. VEGF-A is a 45 kDa glycoprotein homodimer and plays a key role in chemotaxis and angioblast differentiation, endotheliocyte (EC) proliferation, vasculogenesis, and vascular remodeling. As a result of alternative splicing or proteolytic cleavage, 4 main isoforms of VEGF-A are formed, consisting of 121, 165, 189, or 206 amino acid residues.

Green fluorescent protein (GFP) isolated from the jellyfish species Aequorea Victoria, consists of 238 amino acids with a molecular weight of about 27 kDa. GFP is characterized by two absorption peaks in blue light at 395 nm (major) and 475 nm (minor) and a fluorescence peak at 498 nm in the green range. At present, the gene for this protein and proteins derived from it, glowing with different colors, is used as a luminous marker in cell and molecular biology to study protein expression in cells and living organisms in vivo. GFP also allows purification of recombinant proteins, where GFP or its derivatives are used as an affinity label.