Human FGF Basic ELISA Kit

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Cat: abs510023

Size: 96T

Human FGF basic ELISA Kit

Testing Principle

The enzyme immunoassay technique utilized in this kit is quantitative sandwich-based, employing a specific anti-human FGF basic antibody that has been pre-coated on a plate with high affinity. To perform the assay, standards, test samples, and biotinylated detection antibodies are introduced into the wells of an enzyme-labeled plate. Following an incubation period, any FGF basic present in the samples binds to the solid-phase antibodies and the detection antibodies, resulting in the formation of immune complexes. To eliminate any unbound material, the plate is thoroughly washed, and subsequently, horseradish peroxidase-labeled streptavidin (HRP) is added. Another round of washing is performed, and a chromogenic substrate is then introduced, causing the development of color within the darkened environment. To halt the reaction, a stop solution is added, and the absorbance is subsequently measured at a wavelength of 450 nm. It is important to mention that the absorbance measurement is referenced against correction wavelengths of either 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:

The product mentioned is a 96-well polystyrene microplate that has been coated with a capture antibody. It also includes a standard and a detection antibody. Additionally, there is a 10x reagent diluent and a color reagent consisting of two parts, A and B. To facilitate washing, a 25x wash buffer is provided. The ELISA kit is completed with a stop solution and ELISA plate sealers. These product specifications outline the components included in the kit.

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 called FGF-2 or HBGF-2, is a well-studied member of the FGF family that comprises 22 mitogenic proteins. These proteins share 35-60% amino acids, but the acidic and alkaline types do not contain signal peptides and are secreted by an alternative pathway. FGF basic is a subtype that weighs 18 kDa and can be found in the cytoplasm and nucleus, as well as secretory. It might be present in storage tanks of heparin sulphate proteoglycans within or on the surface of the cell. Transcription from alternate initiation sites produces a 21-23 kDa form that is located only in the nucleus.

Both human FGF basic sequences at 18 kDa exhibited high levels of amino acid homology, with around 97% and 99% similarity with mouse/rat and cattle/sheep FGF basic sequences, respectively. However, it was observed that when basic FGF genes were destroyed in mice, the resulting phenotypes were relatively mild in terms of cardiovascular, skeletal, and neurodevelopmental effects. This suggests that other FGF family members may have provided compensation for the loss of basic FGF. Furthermore, transgenic overexpression of basal FGF mainly affected bone development and mineralization.

The differential binding of FGF basic and its splicing variants to four FGF tyrosine kinase receptors (FGF R) has been observed. FGF R1c and 2C exhibit a strong affinity for FGF basic, with picomolar binding. In addition to these receptors, FGF basic has several other binding partners that can modulate its activity in a location- and quantity-dependent manner. These partners 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. These molecules can function as co-receptors or adhesion chaperones on the cell surface, or as bait or reservoirs within the extracellular matrix. They can also act as scavengers or chaperones in the form of free proteins. Notably, the binding of FGF basic to cell surface HSPG is crucial for its interaction with FGF R, including dimerization and activation.

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.

Technical hints: For research use only, not for in vitro diagnosis.

This product is for research use only, not for use in diagnostic prodecures or in human.

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