Description
Principle of the Assay: This assay employs the competitive enzyme immunoassay technique. The microtiter plate provided in this kit has been pre-coated with goat-anti-rabbit antibody. Standards or samples are added to the appropriate microtiter plate wells with an antibody specific for FSH and Horseradish Peroxidase (HRP) conjugated FSH. The competitive inhibition reaction is launched between with HRP labeled FSH and unlabeled FSH with the antibody. A substrate solution is added to the wells and the color develops in opposite to the amount of FSH in the sample. The color development is stopped and the intensity of the color is measured.
Background: Follicle-stimulating hormone (FSH) is a hormone found in humans and other animals. It is synthesized and secreted by gonadotrophs of the anterior pituitary gland. FSH regulates the development, growth, pubertal maturation and reproductive processes of the body. FSH and luteinizing hormone (LH) act synergistically in reproduction. FSH is a 35.5 kDa glycoprotein heterodimer, consisting of two polypeptide units, alpha and beta. Its structure is similar to those of luteinizing hormone (LH), thyroid-stimulating hormone (TSH), and human chorionic gonadotropin (hCG). The alpha subunits of the glycoproteins LH, FSH, TSH, and hCG are virtually identical and consist of about 96 amino acids, while the beta subunits vary. Both subunits are required for biological activity. FSH has a beta subunit of 111 amino acids (FSH beta), which confers its specific biologic action, and is responsible for interaction with the follicle-stimulating hormone receptor. The sugar portion of the hormone is covalently bonded to asparagine, and is composed of N-acetylgalactosamine, mannose, N-acetylglucosamine, galactose, and sialic acid, the last one being critical for its biological half-life of 3-4 hours