GenScript Biotech

Platelet-Derived Growth Factor-BB (PDGF-BB) is one of five dimers (PDGF-AA, AB, BB, CC, and DD) formed by 4 different PDGF subunits. In vivo, PDGF-BB is mainly produced in heart and placenta, and predominantly expressed by osteoblasts, fibroblasts, smooth muscle cells, and glial cells. An inactive precursor of PDGF-BB is produced in the endoplasmic reticulum and then activated by a proprotein convertase after secretion. PDGF-BB functions in a paracrine manner and promotes organogenesis, human skeletal development, and wound healing. PDGF-BB also promotes angiogenesis, particularly in the presence of Fibroblast Growth Factor basic. Therefore, PDGF-BB and its related pathways are potential pharmacological targets.

Platelet-Derived Growth Factor-BB (PDGF-BB) is one of five dimers (PDGF-AA, AB, BB, CC, and DD) formed by 4 different PDGF subunits. In vivo, PDGF-BB is mainly produced in heart and placenta, and predominantly expressed by osteoblasts, fibroblasts, smooth muscle cells, and glial cells. An inactive precursor of PDGF-BB is produced in the endoplasmic reticulum and then activated by a proprotein convertase after secretion. PDGF-BB functions in a paracrine manner and promotes organogenesis, human skeletal development, and wound healing. PDGF-BB also promotes angiogenesis, particularly in the presence of Fibroblast Growth Factor basic. Therefore, PDGF-BB and its related pathways are potential pharmacological targets.

Platelet-Derived Growth Factor-BB (PDGF-BB) is one of five dimers (PDGF-AA, AB, BB, CC, and DD) formed by 4 different PDGF subunits. In vivo, PDGF-BB is mainly produced in heart and placenta, and predominantly expressed by osteoblasts, fibroblasts, smooth muscle cells, and glial cells. An inactive precursor of PDGF-BB is produced in the endoplasmic reticulum and then activated by a proprotein convertase after secretion. PDGF-BB functions in a paracrine manner and promotes organogenesis, human skeletal development, and wound healing. PDGF-BB also promotes angiogenesis, particularly in the presence of Fibroblast Growth Factor basic. Therefore, PDGF-BB and its related pathways are potential pharmacological targets.

Platelet-Derived Growth Factor-BB (PDGF-BB) is one of five dimers (PDGF-AA, AB, BB, CC, and DD) formed by 4 different PDGF subunits. In vivo, PDGF-BB is mainly produced in heart and placenta, and predominantly expressed by osteoblasts, fibroblasts, smooth muscle cells, and glial cells. An inactive precursor of PDGF-BB is produced in the endoplasmic reticulum and then activated by a proprotein convertase after secretion. PDGF-BB functions in a paracrine manner and promotes organogenesis, human skeletal development, and wound healing. PDGF-BB also promotes angiogenesis, particularly in the presence of Fibroblast Growth Factor basic. Therefore, PDGF-BB and its related pathways are potential pharmacological targets.

Platelet-Derived Growth Factor-BB (PDGF-BB) is one of five dimers (PDGF-AA, AB, BB, CC, and DD) formed by 4 different PDGF subunits. In vivo, PDGF-BB is mainly produced in heart and placenta, and predominantly expressed by osteoblasts, fibroblasts, smooth muscle cells, and glial cells. An inactive precursor of PDGF-BB is produced in the endoplasmic reticulum and then activated by a proprotein convertase after secretion. PDGF-BB functions in a paracrine manner and promotes organogenesis, human skeletal development, and wound healing. PDGF-BB also promotes angiogenesis, particularly in the presence of Fibroblast Growth Factor basic. Therefore, PDGF-BB and its related pathways are potential pharmacological targets.

Platelet-Derived Growth Factor-BB (PDGF-BB) is one of five dimers (PDGF-AA, AB, BB, CC, and DD) formed by 4 different PDGF subunits. In vivo, PDGF-BB is mainly produced in heart and placenta, and predominantly expressed by osteoblasts, fibroblasts, smooth muscle cells, and glial cells. An inactive precursor of PDGF-BB is produced in the endoplasmic reticulum and then activated by a proprotein convertase after secretion. PDGF-BB functions in a paracrine manner and promotes organogenesis, human skeletal development, and wound healing. PDGF-BB also promotes angiogenesis, particularly in the presence of Fibroblast Growth Factor basic. Therefore, PDGF-BB and its related pathways are potential pharmacological targets.

Platelet-Derived Growth Factor (PDGF) is a potent mitogen for a wide range of cell types including fibroblasts, smooth muscle, connective tissue, bone and cartilage cells, and some blood cells. The PDGF is involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. The PDGF family consists of proteins derived from four genes (PDGF -A, -B, -C, and -D) that form four disulfide-linked homodimers (PDGF-AA, -BB, -CC, and -DD) and one heterodimer (PDGF-AB).

Platelet-Derived Growth Factor (PDGF) is a potent mitogen for a wide range of cell types including fibroblasts, smooth muscle, connective tissue, bone and cartilage cells, and some blood cells. The PDGF is involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. The PDGF family consists of proteins derived from four genes (PDGF -A, -B, -C, and -D) that form four disulfide-linked homodimers (PDGF-AA, -BB, -CC, and -DD) and one heterodimer (PDGF-AB).

PDGF-DD, also known as platelet-derived growth factor D, IEGF and SCDGFB, is asecreted growth factor belonging to the PDGF/VEGFfamily. It is highly expressed in the heart, pancreas, adrenal glands and ovary. PDGF-DD forms functional homodimers that bind and induce PDGF Rβ homodimers and PDGF Rα/β heterodimers that promote intracellular signaling. This plays an important role in the regulation of cell differentiation, migration and survival. It has also been reported that PDGF-DD can induce monocyte and macrophage recruitment, increase interstitial pressure and facilitate wound healing.

PDGF-DD, also known as platelet-derived growth factor D, IEGF and SCDGFB, is asecreted growth factor belonging to the PDGF/VEGFfamily. It is highly expressed in the heart, pancreas, adrenal glands and ovary. PDGF-DD forms functional homodimers that bind and induce PDGF Rβ homodimers and PDGF Rα/β heterodimers that promote intracellular signaling. This plays an important role in the regulation of cell differentiation, migration and survival. It has also been reported that PDGF-DD can induce monocyte and macrophage recruitment, increase interstitial pressure and facilitate wound healing.

PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is a 50 kDa glycoprotein produced and secreted in many tissues throughout the body. A major component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. In addition, PEDF is able to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuroprotective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recent identification of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities implicate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF also has the potential to be useful in the treatment of various angiogenesis-related diseases including a number of cancers.

PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is a 50 kDa glycoprotein produced and secreted in many tissues throughout the body. A major component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. In addition, PEDF is able to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuroprotective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recent identification of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities implicate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF also has the potential to be useful in the treatment of various angiogenesis-related diseases including a number of cancers.

Platelet factor 4, also known as CXCL4, is expressed in megakaryocytes and stored in the α-granules of platelets. Recombinant human PF-4 is a 7.8 kDa protein containing 70 amino acid residues, including the four highly conserved residues present in CXC chemokines. Platelet factor 4 can be antiproliferative and antiangiogenic, at least in part via interfering with FGF2 and VEGF heparin binding and thus inhibiting their signaling. However, it can also be proinflammatory and proatherogenic through multiple effects on monocytes, macrophages and endothelial cells.

Platelet factor 4, also known as CXCL4, is expressed in megakaryocytes and stored in the α-granules of platelets. Recombinant human PF-4 is a 7.8 kDa protein containing 70 amino acid residues, including the four highly conserved residues present in CXC chemokines. Platelet factor 4 can be antiproliferative and antiangiogenic, at least in part via interfering with FGF2 and VEGF heparin binding and thus inhibiting their signaling. However, it can also be proinflammatory and proatherogenic through multiple effects on monocytes, macrophages and endothelial cells.