One of the most prevalent disorders of man is the dietary deficiency of iron and the resulting anemia. Therefore, the assays of iron, total iron binding capacity and other assessments of iron compounds in the body are clinically significant. Iron-storage compounds in the body include hemoglobin, hemosiderin, myoglobulin and the cytochromes. In most tissues, ferrrtin is a major iron-storage protein. Human ferritin has a molecular weight of approximately 450,000 daltons, and consists of a protein shell around an iron core; each molecule of ferritin may contain as many as 4,000 iron atoms. Under normal conditions, this may represent 25% of the total iron found in the body. In addition, ferrritin can be found in several isomers. High concentrations of ferritin are found in the cytoplasm of the reticuloendothelial system, the liver, spleen and bone marrow. Methods previously used to measure iron in such tissues are invasive, cause patient trauma and lack adequate sensitivity. The measurement of ferritin in serum is useful in determining changes in body iron storage, and is noninvasive with relatively little patient discomfort. Serum ferritin levels can be measured routinely and are particularly useful in the early detection of iron-deficiency anemia in apparently healthy people. Serum ferritin measurements arre also clinically significant in the monitoring of the iron status of pregnant women, blood donors, and renal dialysis patients. High ferritin levels may indicate iron overload without apparent liver damage, as may be noted in the early stages of idiopathic hemochromatosis. Ferritin levels in serum have also been used to evaluate clinical conditions not related to iron storage, including inflammation, chronic liver disease, and malignancy. The Ferritin Enzyme Immunoassay Test Kit provides a rapid, sensitive and reliable assay. The antibodies developed for the test will determine a minimal concentration of human ferritin of 5 ng/ml. There is minimal cross-reativity with human serum albumin, alpha-fetoprotein, human hemoglobin, human transferrin, and ferric chloride.
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Background
With the molecular formula C15H12I3NO4, triiodothyronine (T3) is an active thyroid hormone released by the thyroid gland. T3's chemical structure is made up of three iodine atoms at positions 3, 5, and 3' on the benzene ring as well as a tyrosine derivative. The absence of an iodine atom at the 5' position in the T3 molecule as opposed to thyroxine (T4) greatly increases T3's biological activity. High lipophilicity, which enables it to cross cell membranes and attach to intracellular thyroid hormone receptors (TR), is one of T3's key properties in controlling metabolism. T3 also affects gene expression and metabolic processes.
Thyroid glands produce most of the T3 that is produced, however deiodinases can also convert T4 in peripheral tissues to produce some T3. The majority of T3 in the bloodstream is attached to plasma proteins, specifically thyroxine-binding globulin (TBG). Only a tiny amount of T3 is free in the bloodstream, and it is this free T3 that has biological activity. T3 is carried by the blood to different parts of the body, where it attaches itself to target cell TR receptors to control a number of physiological processes. Furthermore, the hypothalamic-pituitary-thyroid (HPT) axis controls T3 secretion and uses feedback processes to keep the body's T3 levels stable.
T3 helps to maintain appropriate metabolism, cardiac function, body temperature regulation, and growth and development. It regulates gene expression, which affects protein synthesis, fat breakdown, and glucose metabolism and thus the body's overall energy balance. T3 is also required for nervous system growth and maintenance, especially during the central nervous system's formation. Low T3 syndrome models reveal that low T3 levels affect gene expression in cardiomyocytes and diminish myocardial contractility, whereas T3 supplementation restores normal cardiac function. Abnormal T3 levels are linked to a variety of conditions, including hypothyroidism and heart failure. The pathophysiological mechanisms underlying low circulating T3 are not fully understood but may either be a marker of disease severity or lead to impaired cardiovascular function. Moreover, T3 has important applications in medical research and clinical practice, such as diagnosing thyroid dysfunction, studying metabolic diseases, developing drugs, and in certain weight management studies. Overall, the role of T3 in physiological functions and disease regulation is indispensable, and its research and application hold a significant position in the biomedical field.
Alternative Names
T3 [HRP] Conjugate Triiodothyronine (T3) Horseradish Peroxidase Conjugate HRP-Conjugated T3
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