Pigment epithelium-derived factor (PEDF, Serpin-F1, EPC-1) Human,
Rabbit Polyclonal Antibody

Research topic

Others

Introduction to the Molecule

PEDF is syntetized and released by human fetal retinal pigment epithelial cells (RPE) into the interphotoreceptor matrix and is localized to human chromosome 17p. It is a 50 kDa multifunctional glycoprotein belonging to the serpin protease inhibitor supergene (serpin) family, acting like substrates rather than inhibitors of serine proteases, being also described as 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. Interactions of PEDF with three different types of molecules have been discovered: glycosaminoglycans of extracellular matrixes, collagens and receptors on the surface of neuronal cells. Negatively charged, acidic PEDF binds to collagen, lacks neurotrophic activity, and may confer antiangiogenic properties. PEDF has gliastatic, neuronotrophic, neuroprotective and antitumorigenic properties. PEDF 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), identified on Y-79 cells (retinoblastoma cells), cerebellar and motor neurons, and in neural retina and 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.

Note

This product is for research use only.

Source of Antigen

E. coli

Host

Rabbit

Preparation

The antibody was raised in rabbits by immunization with the recombinant Human PEDF.

Amino Acid Sequence

Species Reactivity

Human
Not yet tested in other species.

Purification Method

Immunoaffinity chromatography on a column with immobilized recombinant Human PEDF.

Antibody Content

0.1 mg (determined by BCA method)

Formulation

The antibody is lyophilized in 0.05 M phosphate buffer, 0.1 M NaCl, pH 7.2, AZIDE FREE.

Reconstitution

Add 0.1 ml of deionized water and let the lyophilized pellet dissolve completely. Slight turbidity may occur after reconstitution, which does not affect activity of the antibody. In this case clarify the solution by centrifugation.

Storage/Stability

The lyophilized antibody remains stable and fully active until the expiry date when stored at –20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles and store frozen at –80°C. Reconstituted antibody can be stored at 4°C for a limited period of time; it does not show decline in activity after one week at 4°C.

Quality Control Test

Indirect ELISA – to determine titer of the antibody
SDS PAGE – to determine purity of the antibody

Applications

ELISA, Western blotting

References

• Simonovic M, Gettins PG, Volz K. Crystal structure of human PEDF, a potent anti-angiogenic and neurite growth-promoting factor.
• Becerra SP, Palmer I, Kumar A, Steele F, Shiloach J, Notario V, Chader GJ. Overexpression of fetal human pigment epithelium-derived factor in Escherichia coli. A functionally active neurotrophic factor.
• Gettins PG, Simonovic M, Volz K. Pigment epithelium-derived factor (PEDF), a serpin with potent anti-angiogenic and neurite outgrowth-promoting properties.
• Becerra SP, Sagasti A, Spinella P, Notario V. Pigment epithelium-derived factor behaves like a noninhibitory serpin. Neurotrophic activity does not require the serpin reactive loop.
• Petersen SV, Valnickova Z, Enghild JJ. Pigment-epithelium-derived factor (PEDF) occurs at a physiologically relevant concentration in human blood: purification and characterization.
• Stratikos E, Alberdi E, Gettins PG, Becerra SP. Recombinant human pigment epithelium-derived factor (PEDF): characterization of PEDF overexpressed and secreted by eukaryotic cells.

By research topic:

• Others

By molecule:

• Pigment epithelium-derived factor