Placenta Growth Factor 1 (PIGF-1) (Active) Protein
Quick Overview for Placenta Growth Factor 1 (PIGF-1) (Active) Protein (ABIN7866429)
Target
Protein Type
Biological Activity
Origin
Source
Purity
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Purpose
- Recombinant Human PlGF-1 Protein
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Sequence
- LPAVPPQQWA LSAGNGSSEV EVVPFQEVWG RSYCRALERL VDVVSEYPSE VEHMFSPSCV SLLRCTGCCG DENLHCVPVE TANVTMQLLK IRSGDRPSYV ELTFSQHVRC ECRPLREKMK PERCGDAVPR R
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Specificity
- Chromosomal location:2p21-p16
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Characteristics
- Length (aa):131
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Application Notes
- Measured by its ability to bind to immobilized rh-sFlt-1 in a functional ELISA. Recombinant human PlGF-1 can bind to immobilized rh-sFlt-1 (100 ng/well) with a linear range at 0.5 - 10 ng/mL.
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Restrictions
- For Research Use only
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Format
- Lyophilized
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Reconstitution
- 50 mM acetic acid,Centrifuge vial prior to opening. The PlGF-1 is supplied in lyophilized form with carrier-protein (BSA) and can be reconstituted with 50 mM acetic acid or PBS/water. This solution can be diluted into other buffered solutions or stored frozen for future use.
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Buffer
- 50 mM acetic acid
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Handling Advice
- Avoid repeated freeze-thaw cycles. Centrifuge vial prior to opening
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Storage
- -20 °C,-80 °C
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Storage Comment
- The lyophilized human PlGF-1, though stable at room temperature, is best stored in working aliquots at -20°C to -70°C. Avoid repeated freeze-thaw cycles.
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- Placenta Growth Factor 1 (PIGF-1)
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Alternative Name
- PlGF-1
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Background
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Synonyms: PlGF, placental growth factor
Description: Human Placenta Growth Factor-1 (PlGF-1), a 19 kDa protein consisting of 131 amino acid residues is produced as a homodimer. Human Placenta Growth Factor (PlGF) is a polypeptide growth factor and a member of the platelet-derived growth factor family but more related to vascular endothelial growth factor (VEGF). PlGF-1 acts only as a very weak mitogen for some endothelial cell types and as a potent chemoattractant for monocytes. The physiological function in vivo is still controversial. In several reports it was shown not to be a potent mitogen for endothelial cells and not angiogenic in vivo by using different assays. Very recently it was shown by one investigator, that PlGF-1 from cell culture supernatants was angiogenic in the CAM assay and in the rabbit cornea assay. At least one high-affinity receptor for PlGF (FLT-1 or VEGF-R1) has been demonstrated in different primary cell types (e.g. human umbilical vein endothelial cells and monocytes) but PlGF does not bind to KDR/flk-1. Two different proteins can be generated by differential splicing of the human PlGF gene: PlGF-1 (131 aa native chain) and PlGF-2 (152 aa native chain). Both mitogens are secretable proteins, but PlGF-2 can bind to heparin with high affinity. PlGF-1 is a homodimer, but preparations of PlGF show some heterogeneity on SDS gels depending of the varying degrees of glycosylation. All dimeric forms posses a similar biological profile. There is good evidence that heterodimeric molecules between VEGF and PlGF exists and that they are biological active. Different cells and tissues (e.g. placenta) express PlGF-1 and PlGF-2 at different rates. A very related protein of PlGF is VEGF with about 53 % homology and VEGF-B with similar biological activities.
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Molecular Weight
- ~ 34.0 kDa
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Gene ID
- 5228
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NCBI Accession
- NM_001207012, NP_001193941
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UniProt
- P49763
Target
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