PEDF Human, HEK

Pigment Epithelium-Derived Factor Human Recombinant, HEK
Cat. No.
BT11602
Source
HEK 293.
Synonyms
Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

PEDF Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing a total of 410 amino acids, having a molecular mass of 45.6 kDa and fused to an 11 aa FLAG tag at C-Terminus.
The Human PEDF is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Pigment epithelium-derived factor (PEDF) is a neurotrophic factor with potent anti-angiogenic properties. It is a member of the serpin family, but unlike most serpins, it lacks serine protease inhibitory activity. PEDF plays a crucial role in ocular health by inhibiting the formation of new blood vessels in the eye, a process called angiogenesis. Elevated levels of PEDF are associated with a reduced risk of diabetic retinopathy, a complication of diabetes that can lead to vision loss. PEDF has also been implicated in various other biological processes, including neuronal survival, tumor suppression, and inflammation.
Description
Recombinant human PEDF protein expressed in HEK cells. This protein is a single, glycosylated polypeptide chain comprising 410 amino acids with a molecular weight of 45.6 kDa. An 11 amino acid FLAG tag is fused to the C-terminus of the protein. The protein is purified using proprietary chromatographic techniques to ensure high purity.
Physical Appearance
Sterile white powder obtained by lyophilization (freeze-drying).
Formulation
The protein solution, after filtration through a 0.4 μm filter and concentration to 0.5 mg/ml, was lyophilized in a buffer solution containing 20 mM Tris and 20 mM NaCl at pH 7.5.
Solubility
To prepare a working solution, it is recommended to reconstitute the lyophilized protein in deionized water to a final concentration of 0.5 mg/ml. Ensure complete dissolution of the lyophilized pellet. Please note that the product is not sterile; it is essential to filter the reconstituted protein solution using an appropriate sterile filter before using it in cell culture.
Stability
For long-term storage, keep the lyophilized protein at -20°C. Once reconstituted, aliquot the protein solution and store at 4°C to minimize repeated freeze-thaw cycles. The reconstituted protein is stable at 4°C for a limited period.
Purity
The purity of the protein is determined to be greater than 95% by SDS-PAGE analysis.
Synonyms
Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
Source
HEK 293.
Amino Acid Sequence
QNPASPPEEG SPDPDSTGAL VEEEDPFFKV PVNKLAAAVS NFGYDLYRVR SSTSPTTNVL LSPLSVATAL SALSLGAEQR TESIIHRALY YDLISSPDIH GTYKELLDTV TAPQKNLKSA SRIVFEKKLR IKSSFVAPLE KSYGTRPRVL TGNPRLDLQE INNWVQAQMK GKLARSTKEI PDEISILLLG VAHFKGQWVT KFDSRKTSLE DFYLDEERTV RVPMMSDPKA VLRYGLDSDL SCKIAQLPLT GSMSIIFFLP LKVTQNLTLI EESLTSEFIH DIDRELKTVQ AVLTVPKLKL SYEGEVTKSL QEMKLQSLFD SPDFSKITGK PIKLTQVEHR AGFEWNEDGA GTTPSPGLQP AHLTFPLDYH LNQPFIFVLR DTDTGALLFI GKILDPRGPA AADYKDDDDK.

Product Science Overview

Discovery and Structure

PEDF was first discovered in the late 1980s by Joyce Tombran-Tink and Lincoln Johnson while studying human retinal cell development . The protein is encoded by the SERPINF1 gene located on chromosome 17p13 in humans . PEDF is a 50 kDa glycoprotein composed of 418 amino acids, with a tertiary structure that includes ten α-helices and three β-sheets .

Biological Functions

PEDF is known for its anti-angiogenic, anti-tumorigenic, and neurotrophic functions . It plays a crucial role in various physiological processes, including:

  • Inhibition of Angiogenesis: PEDF reduces the production of vascular endothelial growth factor (VEGF), a potent pro-angiogenic factor, thereby inhibiting the formation of new blood vessels .
  • Neuroprotection: PEDF promotes the survival and differentiation of neurons, making it a potential therapeutic agent for neurodegenerative diseases .
  • Anti-Tumorigenic Activity: PEDF has been shown to suppress tumor growth and metastasis in various cancer models .
Therapeutic Potential

Due to its wide range of biological activities, PEDF is being researched as a therapeutic candidate for several conditions, including:

  • Choroidal Neovascularization: PEDF’s anti-angiogenic properties make it a potential treatment for diseases characterized by abnormal blood vessel growth in the eye .
  • Bone Regenerative Therapy: PEDF promotes mesenchymal stem cell commitment to osteoblasts, increases matrix mineralization, and enhances osteoblast proliferation, making it a promising agent for bone regenerative therapies .
  • Cancer Treatment: PEDF’s ability to inhibit angiogenesis and tumor growth suggests its potential as a therapeutic agent for various cancers .
Human Recombinant PEDF (HEK)

Human recombinant PEDF produced in HEK (Human Embryonic Kidney) cells is a glycosylated polypeptide chain containing 410 amino acids, with a molecular mass of approximately 45.6 kDa . This recombinant form is purified using proprietary chromatographic techniques to ensure high purity and activity .

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