Anti-Glutathione S-Transferase Pi (GST Pi)


Glutathione S-transferases (GSTs) are a group of enzymes centrally involved with drug metabolism and detoxification. Because of their role in detoxification, they have been implicated in anticancer drug sensitivity and resistance. The glutathione S-transferases (GSTs) are a multigene family of isoenzymes which catalyse the conjugation of glutathione to electrophilic substrates. All eukaryotic species possess multiple cytosolic and membrane-bound GST isoenzymes, each of which displays distinct catalytic as well as noncatalytic binding properties. The cytosolic enzymes are encoded by at least five distantly related gene families (designated class alpha, mu, pi, sigma, and theta GST), whereas the membrane-bound enzymes, microsomal GST and leukotriene C4 synthetase, are encoded by single genes and both have arisen separately from the soluble GST. The pi class is found in a wide variety of normal human tissues, including kidney collecting ducts and distal convoluted tubules; urinary, digestive tract and digestive gland epithelium; Schwann and glial cells; lymph node germinal centers; and the endothelium and smooth muscle of blood vessels. In addition, it is also found in multiple structures in the reproductive and endocrine systems, among which are the adrenal cortex and medulla, thyroid follicle cells, ovarian follicles, breast acinar and ductal epithelium, testis epididymis and prostate glandular epithelium and smooth muscle. It is thought that the concentration of GST isoenzymes may play an important role both in the susceptibility of normal tissue to chemotoxins and carcinogens
Intended Use: IVD
Antibody Type: Polyclonal
Clone: Polyclonal
Source: Rabbit
Tissue Type/Cancer Type: Breast