Anti-Gstp1 Antibody serum, from rabbit

Glutathione S-transferase P (EC 2.5.1.18; UniProt P04906; also known as Chain 7, GST 7-7, GST class-pi) is encoded by the Gstp1 gene (Gene ID 24426) in rat species. Glutathione S-transferases constitute a family of metabolic isozymes that are involved in detoxification by catalyzing the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates. The GST family can be subdivided into the cytosolic, mitochondrial, and microsomal (a.k.a. MAPEG) proteins. Mammalian GSTs exist as either homodimers or heterodimers. The individual monomers were historically characterized by their quaternary structure and size, Yf (Mr 24.5 kDa), Yk (25 kDa), Ya1 (25.5 kDa), Ya2 (25.5 kDa), Yn (26.5 kDa), Yb1 (27 kDa), Yb2 (27 kDa) and Yc (28.5 kDa). The Y designation refers to the Y fraction (as apposed to the X and Z fractions) they were found in during purification by Sephadex G75 chromatography. Two GST superfamilies exist that comprise either cytosolic or membrane-bound proteins. Evidence suggests that cytosolic GST increases bodily resistance to carcinogens, products of oxidative stress, environmental pollutants and certain anti-cancer drugs. The cytosolic GSTs are further subdivided into eight classes. namely alpha (GSTA), mu (GSTM), pi (GSTP), sigma, theta (GSTT), kappa (GSTK), zeta (GSTZ), and omega (GSTO). GSTP exists as a homodimer composed of two Yf subunits.