Human FGF Acidic ELISA Kit

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Cat: abs510022

Size: 96T

Human FGF acidic ELISA Kit

Testing Principle

The method employed in this kit is a quantitative sandwich enzyme immunoassay technique. It involves utilizing a high affinity plate coated with a specific anti-human FGF acidic antibody. Into the wells of the enzyme-labeled plate, standards, test samples, and biotinylated detection antibodies are introduced. Following an incubation period, the FGF acidic present in the samples binds with the solid-phase antibodies and the detection antibodies, resulting in the formation of immune complexes. Unbound substances are later washed away, and horseradish peroxidase-labeled streptavidin (HRP) is added. Washing is repeated, and then a chromogenic substrate is introduced. As a result, the color develops in a dark environment. The reaction is halted by adding a stop solution, and the absorbance is measured at a wavelength of 450 nm (with a reference correction wavelength 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:

This is a package that includes a 96-well polystyrene microplate coated with a capture antibody, standard, and detection antibody. It also includes 10 times reagent diluent, color reagent A and B, 25 times wash buffer, stop solution, and ELISA plate sealers. All of these components are of high quality and meet the necessary specification requirements. With this kit, you can perform ELISA assays with ease and confidence, producing accurate and reliable results every time.

Sensitivity:   1.19 pg / mL

Detection range:   125 - 8000 pg/mL

Recovery rate:   96-113%

Storage: 2-8 ° C

The standard curve:

Background: FGF acidic

Fibroblast growth factor acid, also known as FGF-1, is a 17-18 kDa polypeptide that is secreted by various cell types. Interestingly, this molecule lacks an obvious signal peptide sequence, indicating that it does not follow the classical ER/Golgi pathway of secretion. Instead, it appears to have a unique secretion pathway that involves heat shock protein, phosphatidylserine, and Synaptotagmin-1. Upon secretion, disulfide bonds join homodimers, which can be disrupted by reductants, leading to the release of bioactive FGF acidic. Another name for this molecule is endothelial cell growth factor (ECGF) or heparin binding growth factor -1 (HBGF-1).

Acidic FGF, unlike FGF-2, has a 5' standby initiation site. A splicing variant of FGF acidic consisting of 60 amino acids has been discovered, which is comprised of the previous 57 amino acids with an added C-terminal amino acid molecule. While this variant can bind to FGF receptors in experiments, it does not activate them. FGF acidic has a nuclear localization sequence consisting of amino acids 21-27. In mice and rats, FGF acidic has 95% amino acid characteristics, while in cows it has 92%.

Cells known to express acidic FGF include mammary epithelial cells and neurons (motor and sensory), skeletal muscle and smooth muscle cells, proximal tubular cells, endothelial cells, macrophages, keratinocytes, and fibroblasts.FGF family has 5 receptors (FGF R1-R5). The first four receptors are transmembrane tyrosine kinase receptors, while FGF R5 is a member of IgSF that does not have a tyrosine kinase domain.Notably, acidic FGF has been reported to bind to FGF receptors 1 to 4, but not FGF R5.Acidic FGF activates tyrosine kinase binding or uses ligand receptor internalized signaling pathways to reach intracellular organelles and nuclei. Receptor activation was associated with concurrent FGF-heparin interactions.Heparin can bind to acidic FGF to inhibit or activate the receptor.When activated, heparin appears to be a central component connecting the two FGF/FGF R complexes. This is an approximation of two FGF R molecules that initiate receptor dimerization and signal transduction. FGF acidic also binds to heparin on the cell surface and is internalized but not activated. FGF acidic is known for its mitotic activity on endothelial cells. Activation and internalization of membrane receptors are necessary for complete mitosis. Other cells proliferating in response to FGF acidic reactions include silky cells, muscle cells, hepatocytes, breast epithelium, and fibroblasts.

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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