anti-GST3/GST pi (human), Rabbit Monoclonal (RM347)

Inhibition of free radicals and the damage they produce is critical for cell survival, particularly in neurons. Glutathione S-transferases (GSTs) are a class of inducible, multifunctional, detoxifying enzymes that catalyze the reduction of hydrophobic electrophiles, like those generated by pesticides and chemotherapeutic compounds. In mammals, six different isoforms alpha, mu, pi, theta, omega, and zeta have been identified. GST-Pi is expressed in many human tissues, particularly in the biliary tree, renal distal convoluted tubules and lungs. GST-Pi overexpression has been observed in many tumors compared with the surrounding normal tissues and in various cancer cell lines resistant to anticancer agents. It has been shown that GST-Pi acts as a regulator of mitogen-activated protein (MAP) kinases. GST-Pi is an endogenous inhibitor of c-Jun NH2-terminal kinase (JNK), mediated by interactions with the NH2-terminal region of the kinase. After oxidative stress, GST-Pi oligomerizes and disassociates from JNK, which then becomes phosphorylated. GST-Pi can also modulate the activation of p38 and extracellular signal-regulated kinase (ERK).