PLGF Human, His
PIGF, PGF, PLGF-1.
Greater than 95.0% as determined by SDS-PAGE.
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Description
PLGF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 19-131) containing 123 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 13.8kDa (calculated).
Product Specs
PLGF, or placental growth factor, is a protein that plays a crucial role in the formation of new blood vessels (angiogenesis). It promotes the growth and movement of endothelial cells, which line the inside of blood vessels. PLGF binds to a specific receptor called VEGFR-1/FLT1, located on the surface of these cells.
Recombinant human PLGF1, expressed in E. coli bacteria, is a single polypeptide chain consisting of 123 amino acids (a.a 19-131). This non-glycosylated protein includes a 10 amino acid His tag at its N-terminal end. The calculated molecular mass of PLGF1 is 13.8kDa.
The lyophilized PLGF1 powder is sterile-filtered (0.4 μm pore size) and obtained by freeze-drying a solution of 0.5mg/ml PLGF1 in phosphate-buffered saline (PBS) containing 5% w/v trehalose, at pH 7.4.
To prepare a working stock solution, add deionized water to the lyophilized PLGF1 pellet to achieve a concentration of approximately 0.5mg/ml. Allow the pellet to dissolve completely. Note: The provided PLGF1 is not sterile. Prior to cell culture use, it is crucial to sterilize the product by passing it through an appropriate sterile filter.
The purity of PLGF1 is determined to be greater than 95.0% by SDS-PAGE analysis.
PIGF, PGF, PLGF-1.
MKHHHHHHAS LPAVPPQQWA LSAGNGSSEV EVVPFQEVWG RSYCRALERL VDVVSEYPSE VEHMFSPSCV SLLRCTGCCG DENLHCVPVE TANVTMQLLK IRSGDRPSYV ELTFSQHVRC ECR.
Product Science Overview
Placental Growth Factor (PlGF) is a member of the vascular endothelial growth factor (VEGF) family, which plays a crucial role in angiogenesis and vasculogenesis. It is primarily involved in the growth and development of blood vessels during embryogenesis and in the placenta during pregnancy. PlGF is also implicated in various pathological conditions, including cancer, ischemic diseases, and inflammatory disorders.
PlGF is a glycoprotein that exists in several isoforms, with PlGF-1 and PlGF-2 being the most studied. These isoforms are produced through alternative splicing of the PlGF gene. PlGF binds to the VEGF receptor-1 (VEGFR-1), also known as Flt-1, which mediates its biological effects. The binding of PlGF to VEGFR-1 stimulates endothelial cell proliferation, migration, and survival, thereby promoting angiogenesis.
Recombinant human PlGF is produced using various expression systems, including Escherichia coli (E. coli) and human embryonic kidney (HEK) cells. The recombinant form is often tagged with a polyhistidine (His) tag to facilitate purification and detection. The His tag is a sequence of histidine residues that binds to metal ions, allowing for easy isolation of the protein using affinity chromatography.
The production of recombinant PlGF involves cloning the PlGF gene into an expression vector, which is then introduced into the host cells. The host cells express the PlGF protein, which is subsequently harvested and purified. The His tag allows for efficient purification using nickel or cobalt affinity columns. The purified recombinant PlGF is then subjected to various quality control tests to ensure its purity, activity, and stability.
Recombinant PlGF has several applications in research and clinical settings:
- Angiogenesis Research: PlGF is used to study the mechanisms of blood vessel formation and to develop therapeutic strategies for diseases involving abnormal angiogenesis.
- Cancer Research: PlGF is investigated for its role in tumor growth and metastasis, and as a potential target for anti-angiogenic therapies.
- Pre-eclampsia Diagnosis: PlGF levels are measured in pregnant women to assess the risk of pre-eclampsia, a condition characterized by high blood pressure and proteinuria.
- Therapeutic Development: Recombinant PlGF is explored as a therapeutic agent for promoting tissue repair and regeneration in ischemic diseases and wound healing.
