VEGF164-2
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Vascular endothelial growth factor (VEGF) is a highly specific mitogen for vascular endothelial cells. Five VEGF isoforms are generated as a result of alternative splicing from a single VEGF gene. These isoforms differ in their molecular mass and in biological properties such as their ability to bind to cell-surface heparan-sulfate proteoglycans. Mouse VEGF164 shares 97% […]
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VEGF164-1
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Vascular endothelial growth factor (VEGF) is a highly specific mitogen for vascular endothelial cells. Five VEGF isoforms are generated as a result of alternative splicing from a single VEGF gene. These isoforms differ in their molecular mass and in biological properties such as their ability to bind to cell-surface heparan-sulfate proteoglycans. Mouse VEGF164 shares 97% […]
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VEGF120-1
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Vascular endothelial growth factor (VEGF) is a highly specific mitogen for vascular endothelial cells. Five VEGF isoforms are generated as a result of alternative splicing from a single VEGF gene. These isoforms differ in their molecular mass and in biological properties such as their ability to bind to cell-surface heparan-sulfate proteoglycans. Mouse VEGF120 shares 98% […]
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VEGF121
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Vascular endothelial growth factor 121 (VEGF121) is a protein that plays a crucial role in the growth and survival of blood vessels. It stimulates the formation of new blood vessels, a process known as angiogenesis, which is essential for normal development and tissue repair. VEGF121 has therapeutic applications for conditions such as ischemic heart disease […]
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VEGF165
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VEGF 165, also known as Vascular Endothelial Growth Factor 165, is a protein that plays a critical role in angiogenesis, the process of forming new blood vessels from pre-existing ones. It belongs to the vascular endothelial growth factor family and is one of the most well-studied isoforms of VEGF. Human VEGF 165 protein is a […]
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IGF-BP7
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IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. Currently, there are seven named IGF-BPs that form high affinity complexes with both IGF-I and IGF-II. IGF-BP7 is expressed in a wide range of normal human tissues, and it generally shows reduced expression in cancer cell lines of prostate, […]
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IGF-BP3
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IGF-BP3 is a 30 kDa, cysteine-rich secreted protein. It is the major IGF binding protein present in the plasma of human and animals, and it is also found in α-granules of platelets. In addition to its ability to modulate the activity of IGF-I and IGF-II, IGF-BP3 exerts inhibitory effects on follicle stimulating hormone (FSH) activity. […]
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IGF-BP4
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IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes […]
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IGF-BP5
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IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. Currently, there are seven named IGF-BPs that form high affinity complexes with both IGF-I and IGF-II. IGF-BP5 is a 28.6 kDa, cysteine-rich, secreted protein produced by vascular smooth muscle cells. It is the major IGF-binding protein present in bone […]
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IGF-1-3
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Insulin-like Growth Factor I (IGF-I), is the dominant effector of Growth Hormone (GH) and is structurally homologous to Proinsulin. The 7.6 kDa mature IGFI is identical between isoforms and is generated by proteolytic removal of the N- and C-terminal regions. Mature human IGF-I shares 94% and 96% amino acid (aa) sequence identity with the mouse […]
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