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Human Recombinant PDGF-CC

Platelet-derived growth factor CC

Human Recombinant PDGF-CC

Platelet-derived growth factor CC

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Platelet-derived growth factor CC
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Overview

The platelet-derived growth factor (PDGF) family has five heparin-binding members that assemble into four homodimers (PDGF-AA, PDGF-BB, PDGF-CC, and PDGF-DD) and one heterodimer (PDGF-AB; Li & Eriksson). PDGF signals through the receptor tyrosine kinases PDGFRα and PDGFRβ. It has been shown that PDGF-induced migration involves signaling pathways involving MEK/ERK, EGFR, Src and PI3K/AKT (Kim et al.). PDGF is a potent mitogen for cells of mesenchymal origin such as fibroblasts and vascular smooth muscle cells. PDGF has been implicated in pathogenesis of atherosclerosis, glomerulonephritis, cancer, and in the contraction of vascular smooth muscle cells of rat aortic tissues (Fretto et al.; Sachinidis et al.). PDGF-CC is secreted as a latent growth factor and requires activation by proteolytic processing (Li & Eriksson). PDGF-CC binds to PDGFRα homodimers and PDGFRαβ heterodimers, but not to PDGFRβ homodimers (Li & Eriksson). PDGF-CC is an angiogenic factor that stimulates coronary artery smooth muscle cell proliferation and plays a role in cardiovascular development (Gilbertson et al.). PDGF-CC is also expressed in many tumors and plays a role in tumorigenesis (Zwerner & May).
Subtype
Cytokines, Growth Factors
Cell Type
Mesenchymal Cells, PSC-Derived, Neural Cells, PSC-Derived, Neural Stem and Progenitor Cells, Neurons, Osteoblasts, Other
Species
Human
Area of Interest
Neuroscience, Stem Cell Biology
Purity
≥ 95%

Data Figures

(A) The biological activity of Human Recombinant PDGF-CC was tested by its ability to promote the proliferation of 3T3 cells. Cell proliferation was measured using a fluorometric assay method. The EC50 is defined as the effective concentration of the growth factor at which cell proliferation is at 50% of maximum. The EC50 in the example above is less than 1 ng/mL. (B) 5 μg of Human Recombinant PDGF-CC was resolved with SDS-PAGE under reducing (+) and non-reducing (-) conditions and visualized by Coomassie Blue staining. Human Recombinant PDGF-CC has a predicted molecular mass of 12.5 kDa.

Protocols and Documentation

Find supporting information and directions for use in the Product Information Sheet or explore additional protocols below.

Document Type
Product Name
Catalog #
Lot #
Language
Document Type
Product Name
Catalog #
78168, 78168.1
Lot #
All
Language
English
Document Type
Product Name
Catalog #
78168, 78168.1
Lot #
All
Language
English

Applications

This product is designed for use in the following research area(s) as part of the highlighted workflow stage(s). Explore these workflows to learn more about the other products we offer to support each research area.

Resources and Publications

Publications (1)

Tissue and Isoform-Specific Effects of Platelet-Derived Growth Factor on Neonatal-Derived Dermal and Fetal-Derived Lung Fibroblast Profibrotic Functions. B. Kohlen et al. Cells 2026 Apr

Abstract

Elevated levels of platelet-derived growth factor (PDGF) isoforms in fibrosis are implicated in driving a dysfunctional profibrotic fibroblast phenotype. This study investigated the differential effects of the five PDGF isoforms (AA, AB, BB, CC, and DD) in inducing neonatal dermal and fetal lung fibroblast contraction, proliferation, cytokine production, myofibroblast differentiation, and extracellular matrix (ECM) deposition. All PDGF isoforms, except PDGF-AA, increased contraction of 3-dimensional collagen I gels by dermal (p < 0.01) and lung fibroblasts (p < 0.05) compared to media control. PDGF-AB, BB, and CC enhanced proliferation only in dermal fibroblasts (p < 0.05). PDGF-BB induced profibrotic IL-11 cytokine release in dermal and lung fibroblasts (p < 0.0001) and IL-6 cytokine release in dermal fibroblasts (p < 0.05) compared to media control. None of the PDGF isoforms affected ECM synthesis or myofibroblast differentiation. Dermal fibroblasts exhibited elevated PDGF Receptor-β (PDGFRβ) expression (p < 0.01) and increased basal ERK1/2 phosphorylation (p < 0.05) compared to lung fibroblasts. In summary, PDGF modulates fibroblast functions in a tissue-specific manner, with PDGF-BB driving profibrotic processes in dermal fibroblasts through high PDGFRβ expression and ERK1/2 signalling. Further research is needed to explore the benefit of tissue and isoform-specific PDGF inhibition strategies in skin and lung fibrosis.