PDGF AA Human

Recombinant human PDGF-AA (hPDGF-AA) is produced in Escherichia coli (E. coli) and is optimized for use in cell culture, differentiation studies, and functional assays . The recombinant protein is highly pure, with a molecular weight of approximately 18 kDa when reduced and 34 kDa when non-reduced . The protein is stable in its lyophilized state at -20°C for up to a year and can be reconstituted with carrier protein for use in various applications .

PDGF-AA is integrally involved in the proliferation and migration of fibroblasts, which are essential for wound healing and tissue repair . It is produced by various cell types, including epithelial, muscle, osteosarcoma, and neuronal progenitor cells . The active form of PDGF-AA is generated through intracellular proteolytic cleavage of a larger precursor .

PDGF-AA binds to the PDGF receptor alpha (PDGFR-α), activating receptor tyrosine kinase and initiating several downstream signaling pathways, including the Ras-MAPK, PI3K/AKT, and PLCγ pathways . These pathways are crucial for cell growth, survival, and migration.

Dysregulation of PDGF-AA expression and signaling is often associated with various diseases, including cancer and fibrotic disorders . Research has shown that PDGF-AA plays a significant role in the development of several cell types and tissues, making it a critical factor in both normal physiology and disease pathology .

Recombinant human PDGF-AA is widely used in research to study mesenchymal cell growth, morphogenesis, and migration . It is also utilized in investigations of PDGFR signaling and angiogenesis . The protein’s high purity and biological activity make it suitable for a variety of cell culture applications and functional assays .