Product name : Human, PEDF , Rec. Prot.
Catalog number : RD172114100
Quantity: 0.1 mg
Supplier name : Biovend
Data sheet : Ask more or other datasheet now !
PEDF is syntetized and released by human fetal retinal pigment epithelial cells (RPE) into the interphotoreceptor matrix. It is localized to the human chromosome 17p. It is a 50 kDa multifunctional glycoprotein belonging to the serpin protease inhibitor supergene (serpin) family. It behaves like a substrate rather than inhibitors of serine proteases. PEDF is a serine peptidase inhibitor, clade F (alfa-2 antiplasmin, pigment epithelium derived factor), member 1. This gene encodes a 418 amino-acid protein with an asparagine glycosylation site at position 285–287 (Asn-Leu-Thr) and N-terminal signal peptide associated with secreted proteins. PEDF has an asymmetrical charge distribution with a high density of basic residues concentrated on one side (positive) of the molecule and of acidic residues on the opposite side. PEDF Interacts with three different types of molecules: glycosaminoglycans of extracellular matrixes, collagens and receptors on the surface of neuronal cells. Acidic PEDF binds to collagen when it is negatively charged. In this scenario it lacks neurotrophic activity and may confer antiangiogenic properties. PEDF has gliastatic, neuronotrophic, neuroprotective and antitumorigenic properties. It acts in neuronal differentiation and survival in cells derived from retina and the central nervous system (CNS).Two functional epitopes have been identified on PEDF: a 34-mer peptide (residues 24–57) and a 44-mer peptide (residues 58–101). 44-mer peptide interacts with a a putative 80 kDa receptor (PEDFRN), which is found on Y-79 cells, cerebellar and motor neurons and in neural retina. This peptide also replicates the neurotrophic function and the ability to block vascular leackage. The 34-mer peptide, possibly via a distinct receptor (PEDF-RA) identified on endothelial cells, induces apoptosis, blocks endothelial cell migration and corneal angiogenesis, but fails to induce Y-79 differentiation. Recently, PEDF was shown also to have potent anti-angiogenic activity as it specifically inhibited the migration of endothelial cells, an essential step in angiogenesis. Its activity equals or supersedes that of other anti-angiogenic factors, including angiostatin, endostatin and thrombospondin-1. In cell culture and in animal models, PEDF inhibited endothelial cell (EC) growth and migration and suppressed ischemia-induced neovascularization, whereas in porcine liver, the expression of PEDF has been associated with body muscularity and obesity. Analyses revealed that Human PEDF is correlated with BMI, CRP, diastolic blood pressure, insulin, Quicki. Individuals with metabolic syndrome (NCEP criterion) have significantly higher PEDF values than healthy subjects , suggesting that PEDF is and independent marker of MS with sufficient diagnostic efficacy.
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