Platelet Derived Growth Factors (PDGF)

By: Jennifer Fries, BioFiles 2009, 4.5, 20.

Platelet-Derived Growth Factor is the principal mitogen found in mammalian serum and is released from platelets during clot formation.1 PDGF elicits multifunctional actions with a variety of cells, including mitogenesis of mesoderm-derived cells, increased extracellular matrix synthesis, and chemotaxis and activation of neutrophils, monocytes and fibroblasts. PDGF is mitogenic for dermal and tendon fibroblasts, vascular smooth muscle cells, glial cells and chondrocytes. PDGF appears to interact with Transforming Growth Factor-1 in accelerating wound healing.2 However, PDGF may also be pathogenic in arteriosclerosis and neoplasia.3 The mitogenic activities of all PDGF products are tested in culture using Swiss 3T3 cells or NR6-3T3 fibroblasts.4

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Platelet Derived Growth Factors (PDGF)

Product Description Source Recombinant Host Physical Form Assay Cell Type Affected Cat. No.
Platelet-Derived Endothelial Cell Growth Factor human Sf21 cells lyophilized powder The proliferative activity of human PD-ECGF is measured in culture by using human umbilical vein endothelial cells. vascular endothelial cell P5208-10UG
Platelet-Derived Growth Factor from human platelets - lyophilized powder The mitogenic activity is tested in culture using Swiss 3T3 cells or NR6-3T3 fibroblasts. chrondrocyte mesenchymal cell fibroblast glial cell muscle cell P8147-1VL
Platelet-Derived Growth Factor from porcine platelets - lyophilized powder The mitogenic activity is tested in culture using Swiss 3T3 cells or NR6-3T3 fibroblasts. glial cell fibroblast mesenchymal cell chrondrocyte muscle cell P8953-5UG

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Platelet Derived Growth Factors - AA (PDGF-AA)

Product Description Source Recombinant Host Physical Form Assay Cell Type Affected Cat. No.
Platelet-Derived Growth Factor-AA human Escherichia coli lyophilized powder The biological activity is measured by the dosedependent stimulation of thymidine uptake by BALB/c 3T3 cells. chrondrocyte glial cell fibroblast mesenchymal cell muscle cell P3076-10UG

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Platelet Derived Growth Factors - AB (PDGF-AB)

Product Description Source Recombinant Host Physical Form Assay Cell Type Affected Cat. No.
Platelet-Derived Growth Factor-AB human Escherichia coli lyophilized powder The biological activity is measured by its ability to stimulate 3H-thymidine incorporation in quiescent NR6R-3T3 fibroblasts. chrondrocyte glial cell fibroblast mesenchymal cell muscle cell P3326-10UG

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Platelet Derived Growth Factors - BB (PDGF-BB)

Product Description Source Recombinant Host Physical Form Assay Cell Type Affected Cat. No.
Platelet-Derived Growth Factor-BB human Escherichia coli lyophilized powder The biological activity is measured by its ability to stimulate 3H-thymidine incorporation in quiescent NR6R-3T3 fibroblasts. fibroblast glial cell muscle cell chrondrocyte mesenchymal cell P3201-10UG
Platelet-Derived Growth Factor-BB from rat Escherichia coli lyophilized powder The biological activity is measured by its ability to stimulate 3H-thymidine incorporation in quiescent NR6R-3T3 fibroblasts. glial cell chrondrocyte muscle cell mesenchymal cell fibroblast P4056-50UG
Platelet-Derived Growth Factor-BB human Escherichia coli lyophilized powder The biological activity is measured by the dosedependent stimulation of thymidine uptake in BALB/c 3T3 cells. glial cell muscle cell chrondrocyte mesenchymal cell fibroblast P4306-10UG

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Materials

     

References

  1. Ross, R., et al., A platelet-dependent serum factor that stimulates the proliferation of arterial smooth muscle cells in vitro. Proc. Natl. Acad. Sci. USA, 71, 1207-1210 (1974).
  2. Pierce, G., et al., Platelet-derived growth factor and transforming growth factor-b enhance tissue repair activities by unique mechanisms. J. Cell. Biol., 109, 429-440 (1989).
  3. Ross, R., Atherosclerosis: a problem of the biology of arterial wall cells and their interactions with blood components. Arteriosclerosis, 1, 293-311 (1981).
  4. Raines, E., et al., Purification of human platelet-derived growth factor. Meth. Enzymol., 109, 749-773 (1985).

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