PDGF-BB Protein, Human, E. coli

PDGF-BB Protein, Human is the most active PDGF isoform, binds to PDGF receptor, promotes diverse cell types proliferation and osteogenesis, and further stimulates bone formation in fracture or defect. PDGF-BB Protein, Human improves collagenase-induced achilles tendinopathy in rats.

Background: Recombinant Human Platelet-derived Growth Factor-BB is the most active PDGF isoform, binds to PDGF receptor, promotes diverse cell types proliferation and osteogenesis, and further stimulates bone formation in fracture or defect. Platelet-derived growth factor-BB (PDGF-BB) is primarily secreted from platelet α-granules and is the most active PDGF isoform in bone and other connective tissue as it can bind to all known PDGF receptors. PDGF-BB plays an important role in bone regeneration by inducing mitogenesis, chemotaxis, extracellular matrix formation, and vascularization. Recombinant Human Platelet-derived Growth Factor-BB (rhPDGF-BB) accelerates tendon healing by improving matrix remodeling, increased collagen synthesis, and increased cell proliferation. Recombinant Human Platelet-derived Growth Factor-BB is also efficacious in a non-ruptured, degenerated, tendinopathy model. Furthermore, Recombinant Human Platelet-derived Growth Factor-BB addresses chronic tendinopathies by inducing proliferation and migration of progenitor cells and tenocytes, which stimulate structural repair of the degenerated tendon.