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Human FGF basic ELISA Kit


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Testing Principle
This kit uses quantitative sandwich enzyme immunoassay technique. A specific anti-human FGF basic antibody is pre-coated on a high affinity plate. Standards, test samples, and biotinylated detection antibodies are added to the wells of the enzyme-labeled plate. After incubation, the FGF basic present in the samples combines with the solid-phase antibodies and the detection antibodies to form immune complexes. After washing to remove unbound material, horseradish peroxidase-labeled streptavidin (HRP) was added. After washing, a chromogenic substrate was added, and the color was developed in the dark. The reaction was stopped by adding a stop solution, and the absorbance was measured at a wavelength of 450 nm (reference correction wavelength of 540 nm or 570 nm).
Detection type: sandwich enzyme immunoassay
Form: pre-coated 96-well plate
Sample type: Cell culture supernatant, Serum, Plasma
Sample quantity: 100ul
Kit composition:
96 well polysyrene microplate coated with capture antibody, standard, detection antibody, 10×reagent diluent, Color reagent (A and B), 25×wash buffer, Stop solution, ELISA plate sealers, specification
Sensitivity: 0.089-0.740 pg / mL
Detection range: 15.6 - 1000 pg/mL
Recovery rate: 94-119%
Storage: 2-8 ° C
The standard curve:
Background: FGF acidic
FGF basic, also known as FGF-2(fibroblast growth factor-2) or HBGF-2(heparin-binding growth factor-2), is the most intensively studied of the 22 mitogenic proteins in the FGF family.FGF family members share 35-60% amino acids (aa), but only acidic and alkaline FGF lack signal peptides,which are secreted by another pathway. The 18 kDa FGF basic subtype can be found in the cytoplasm and nucleus and is also secretory.It may be present in storage tanks of heparin sulphate proteoglycans (HSPG) inside or on the cell surface.Transcription from alternate initiation sites produces a 21-23 kDA form, found only in the nucleus.
Human FGF basic sequences at 18 kDa had aa homology of 97% and 99%, respectively, with mouse/rat and cattle/sheep FGF basic sequences. However, the destruction of basic FGF genes in mice resulted in relatively mild cardiovascular, skeletal, and neurophenotypes, suggesting that other members of the FGF family compensated for this.Transgenic basal overexpression mainly affects bone development and mineralization.
Four FGF tyrosine kinase receptors (FGF R) and their splicing variants showed differential binding of FGF.FGF basic preferentially binds FGF R1c and 2C with picoluminal affinity.FGF basic also has a number of other binding partners that can fine-tune FGF basic activity depending on their location and number. These include heparin, integrin V 3, soluble FGF R1, FGF binding protein, free gangliosides, platelet-reactive protein, pentammeric protein 3, fibrinogen, 2-macroglobulin, platelet-derived growth factor and platelet factor-4, all of which bind in nanomolar affinity. These molecules can act as co-receptors or adhesion chaperones of the cells, bait or reservoir in the extracellular matrix, while scavengers or chaperones can act as free proteins. FGF basic binding to cell surface HSPG is particularly critical and is necessary for binding, dimerization, and activation of FGF R.
FGF basic regulates normal processes such as angiogenesis, wound healing, tissue repair, learning and memory, and embryonic development and differentiation of the heart, bone, and brain.It is upregitated by inflammatory mediators such as TNF-α, IL-1β, IL-2, PDGF and nitric oxide.Many human tumors express basic FGF, which may be related to tumor angiogenesis.