PEDF Human
Pigment Epithelium-Derived Factor Human Recombinant
Cat. No.
BT11540
Source
Escherichia Coli.
Synonyms
Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
Appearance
Sterile 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.
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Description
PEDF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 400 amino acids and having a molecular mass of 44.5 kDa.
The Human PEDF is purified by proprietary chromatographic techniques.
The Human PEDF is purified by proprietary chromatographic techniques.
Product Specs
Introduction
PEDF, Pigment Epithelium-Derived Factor, is a multifaceted protein known for its neurotrophic, anti-angiogenic, and anti-tumorigenic properties. Found abundantly throughout the body, PEDF acts as a natural defense mechanism against uncontrolled blood vessel growth (angiogenesis), a hallmark of many diseases. It achieves this by prompting the self-destruction of proliferating endothelial cells, the building blocks of blood vessels, and by hindering the action of pro-angiogenic factors like VEGF and FGF-2. Furthermore, PEDF exhibits neuroprotective qualities, shielding neurons from damage caused by oxidative stress and excitotoxicity. Its interaction with a specific cell surface receptor, PEDF-R, is key to its multifaceted biological activities. This unique receptor-ligand partnership distinguishes PEDF within the serpin family and offers valuable insights into its mechanisms of action. The remarkable attributes of PEDF have sparked considerable interest in its therapeutic potential for conditions like age-related macular degeneration (AMD) and diabetic retinopathy, where abnormal angiogenesis plays a central role. Moreover, PEDF holds promise as a potential weapon against various cancers, further underscoring its significance in biomedical research.
Description
Recombinant Human PEDF, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 400 amino acids with a molecular weight of 44.5 kDa. It undergoes purification using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The protein solution, concentrated to 1 mg/ml and sterile filtered, was lyophilized with a buffer solution of 20mM sodium phosphate and 150mM NaCl, at a pH of 7.4.
Solubility
To reconstitute the lyophilized PEDF, it is recommended to dissolve it in sterile 18M-cm H₂O at a concentration not less than 100 µg/ml. This solution can then be further diluted into other aqueous solutions as needed.
Stability
Lyophilized PEDF, though stable at room temperature for up to 3 weeks, should ideally be stored desiccated at a temperature below -18°C. After reconstitution, it is advisable to store Human PEDF at 4°C for a period of 2-7 days. For long-term storage, freezing below -18°C is recommended. To enhance stability during long-term storage, consider adding a carrier protein such as 0.1% HSA or BSA. It is crucial to avoid repeated freeze-thaw cycles to maintain protein integrity and activity.
Purity
The purity of the recombinant Human PEDF is determined to be greater than 95% as assessed by SDS-PAGE analysis.
Synonyms
Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
Source
Escherichia Coli.
Amino Acid Sequence
MQNPASPPEE GSPDPDSTGA LVEEEDPFFK VPVNKLAAAV SNFGYDLYRV RSSMSPTTNV LLSPLSVATA LSALSLGAEQ RTESIIHRAL YYDLISSPDI HGTYKELLDT VTAPQKNLKS ASRIVFEKKL RIKSSFVAPL EKSYGTRPRV LTGNPRLDLQ EINNWVQAQM KGKLARSTKE IPDEISILLL GVAHFKGQWV TKFDSRKTSL EDFYLDEERT VRVPMMSDPK AVLRYGLDSD LSCKIAQLPL TGSMSIIFFL PLKVTQNLTL IEESLTSEFI HDIDRELKTV QAVLTVPKLK LSYEGEVTKS LQEMKLQSLF DSPDFSKITG KPIKLTQVEH RAGFEWNEDG AGTTPSPGLQ PAHLTFPLDY HLNQPFIFVL RDTDTGALLF IGKILDPRGP.
Product Science Overview
Discovery and Identification
Structure and Function
PEDF is a 50 kDa secreted glycoprotein that belongs to the serpin (serine protease inhibitor) family, specifically classified as serpin F1. Despite being a serpin, PEDF does not exhibit protease inhibitory activity. Instead, it is known for its anti-angiogenic, anti-tumorigenic, and neurotrophic functions .
Biological Activities
- Anti-Angiogenic Activity: PEDF is a potent inhibitor of angiogenesis, the process of new blood vessel formation. This property makes it a promising therapeutic candidate for diseases characterized by abnormal blood vessel growth, such as age-related macular degeneration (AMD) and certain types of cancer .
- Neurotrophic Effects: PEDF promotes the survival and differentiation of neurons. It has been shown to protect retinal cells from degeneration and is being explored for its potential in treating neurodegenerative diseases .
- Anti-Tumorigenic Properties: PEDF exhibits anti-tumorigenic effects by inhibiting the growth and metastasis of various cancer cells. Its ability to induce apoptosis (programmed cell death) in tumor cells further enhances its therapeutic potential .
Recombinant PEDF
Recombinant PEDF refers to the protein produced through recombinant DNA technology, which allows for the large-scale production of this protein for research and therapeutic purposes. Human recombinant PEDF retains the biological activities of the naturally occurring protein and is used in various experimental and clinical studies .
Therapeutic Potential
Due to its multifunctional nature, PEDF is being investigated for its therapeutic potential in a wide range of conditions, including:
- Ophthalmic Diseases: PEDF’s anti-angiogenic properties make it a candidate for treating diseases like AMD and diabetic retinopathy.
- Cancer: Its ability to inhibit tumor growth and metastasis is being explored in cancer therapy.
- Neurodegenerative Diseases: PEDF’s neuroprotective effects are being studied for potential applications in diseases such as Alzheimer’s and Parkinson’s .
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