Cayman PEDF (human, recombinant)

Pigment epithelium-derived factor (PEDF) is a secreted glycoprotein encoded by the SERPINF1 gene. It is a non-inhibitory member of the serine-protease inhibitor (SERPIN) superfamily that has anti-angiogenic and neurotrophic activities. PEDF is a 418-amino acid protein comprised of an N-terminal region important for its neurotrophic activity, three β-sheets and ten α-helices that make up an α/β core serpin domain, and a C-terminal region containing a glycosylation site.^, It has an asymmetrical charge distribution with the basic region involved in glycosaminoglycan binding and the acidic region binding to collagen I. PEDF is ubiquitously expressed and localized to the extracellular matrix but can also be found in the cytoplasm and nucleus of retinal pigment epithelial cells and certain cancer cell lines.^, It contains biologically active peptides, including a 34-amino acid peptide (amino acids 44-77), which contains a laminin receptor binding site and has anti-angiogenic, bone mineralization, and apoptotic activities, and a 44-amino acid peptide (amino acids 78-121), which contains a PNPLA2 binding site and promotes neuronal differentiation and inhibits vascular permeability.^,, PEDF also interacts with collagen I for its anti-angiogenic activity, as well as with sulfated (heparin) and non-sulfated (hyaluronan) glycosaminoglycans, which are important for PNPLA2 receptor binding and activation of caspases, respectively.^, Its expression is reduced in a variety of cancer cell lines and solid tumors, and the reduction is associated with metastasis and poor prognosis. Mutations in SERPINF1 are responsible for the hereditary bone dysplasia disorder osteogenesis imperfecta type VI, which is characterized by bone fragility, deformity, and growth deficiency. Cayman’s PEDF (human, recombinant) protein consists of 410 amino acids, has a calculated molecular weight of 45.8 kDa, and a predicted N-terminus of Gln20 after signal peptide cleavage.

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