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EK000040-EK0490: Human Placental Growth Factor ELISA Kit
Range 15.6pg/ml-1000pg/ml
Sensitivity < 1 pg/ml
Specificity: no detectable cross-reactivity with any other cytokine.
Application: for quantitive detection of human PLGF in sera, plasma, body fluids, tissue lysates or cell culture supernates.
Expiration: four months at 4°C and eight months at -20°C.
Background
The protein, also called PGF, is 149 amino acids long and shares 53% identity with the platelet-derived growth factor-like region of human VPF. And the N-glycosylated PLGF protein is secreted into the medium and that it functions as a dimer1. The PLGF gene is mapped to 14q24-q31. There are 3 isoforms of PGF, designated PGF1, PGF2, and PGF3. Only PGF2 is able to bind heparin. Additionally, PGF regulates inter- and intramolecular cross-talk between the VEGF receptor tyrosine kinases FLT1 and FLK12. It also can stimulate angiogenesis and collateral growth in ischemic heart and limb with at least a comparable efficiency to VEGF3.
Principle
The ELISA Kit is based on standard sandwich enzyme-linked immune-sorbent assay technology. The target specific antibodies are precoated onto 96-well plates. The target from the sample is bound to the microwell. The biotinylated target specific detection antibodies are added to the microwells and followed by washing with the PBS or TBS buffer. Avidin-Biotin-Peroxidase Complex is added and unbound conjugates are washed away with the PBS or TBS buffer. TMB, the HRP (horseradish peroxidase) substrate, is used to visualize color change resulting from the HRP enzymatic reaction. TMB is catalyzed by HRP to produce the blue color. The color changes into yellow after the acidic stop solution is added. The density of the yellow color is proportional to the target amount from the sample captured in the microwells.
Reference
1. Maglione, D.; Guerriero, V.; Viglietto, G.; Delli-Bovi, P.; Persico, M. G. : Isolation of a human placenta cDNA coding for a protein related to the vascular permeability factor. Proc. Nat. Acad. Sci. 88: 9267-9271, 1991.
2. Autiero, M.; Waltenberger, J.; Communi, D.; Kranz, A.; Moons, L.; Lambrechts, D.; Kroll, J.; Plaisance, S.; De Mol, M.; Bono, F.; Kliche, S.; Fellbrich, G.; and 16 others : Role of PlGF in the intra- and intermolecular cross talk between the VEGF receptors Flt1 and Flk1. Nature Med. 9: 936-943, 2003.
3. PLGF stimulated angiogenesis and collateral growth in ischemic heart and limb with at least a comparable efficiency to VEGF. Luttun, A.; Tjwa, M.; Moons, L.; Wu, Y.; Angelillo-Scherrer, A.; Liao, F.; Nagy, J. A.; Hooper, A.; Priller, J.; De Klerck, B.; Compernolle, V.; Daci, E.; and 10 others : Revascularization of ischemic tissues by PlGF treatment, and inhibition of tumor angiogenesis, arthritis and atherosclerosis by anti-Flt1. Nature Med. 8: 831-840, 2002.
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