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PDGF-AA-1 inquiry  | Purity Not Available

Protheragen

PDGF is involved in a number of biological processes, including hyperplasia, embryonic neuron development, chemotaxis, and respiratory tubule epithelial cell development. The A-chain homodimers of the platelet-derived growth factor (PDGF AA) are widely expressed in normal and transformed cells. The mitogenic properties of PDGF AA are well established. FGF-2 and platelet-derived growth factor-A (PDGF-AA) are […]

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EG-VEGF-1 inquiry  | Purity Not Available

Protheragen

EG-VEGF is a secreted angiogenetic mitogen growth factor expressed in the steroidogenic glands, ovary, testis, adrenal gland, and placenta. EG-VEGF induces proliferation, migration, and fenestration (formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. The human EG-VEGF gene codes for a 105 amino acid polypeptide containing an N-terminal signal sequence of 19 […]

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VEGF120-2 inquiry  | Purity Not Available

Protheragen

Vascular endothelial growth factor (VEGF or VEGF-A)/vascular permeability factor (VPF), is an important signaling protein as a potent mediator of both angiogenesis and vasculogenesis. It is a member of the platelet-derived growth factor (PDGF) family, and characterized by a cysteine-knot structure and disulfide-linked homodimer. Alternately spliced isoforms of 121, 145, 165, 183, 189, and 206 […]

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EG-VEGF-2 inquiry  | Purity Not Available

Protheragen

Endocrine gland-derived vascular endothelial growth factor (EG-VEGF), also called prokineticin 1 (PK1), is a member of the prokineticin family of secreted proteins that share a common structural motif containing ten conserved cysteine residues that form five pairs of disulfide bonds. The mature region in mouse is 93% and 87% aa identical to the mature regions […]

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VEGF120-1 inquiry  | Purity Not Available

Protheragen

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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VEGF164-1 inquiry  | Purity Not Available

Protheragen

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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VEGF164-2 inquiry  | Purity Not Available

Protheragen

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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VEGF165 inquiry  | Purity Not Available

Protheragen

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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VEGF121 inquiry  | Purity Not Available

Protheragen

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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IGF-BP7 inquiry  | Purity Not Available

Protheragen

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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