Anti-GST3/GST pi/GSTP1 Antibody Picoband® Fluoro647 Conjugated

Glutathione S-transferases pi (GSTP1), also known as GST3, is an enzyme that in humans is encoded by the GSTP1 gene. This gene is mapped to 11q13.2. GSTP1 has 7 exons and 6 introns contained within approximately 2.8 kilobases. GSTP1 belongs to Glutathione S-transferases (GSTs) which are a family of enzymes that play an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. GSTP1 presents in all tissues and cells, with the exception of red cells, in which only erythrocyte GST (GSTe) is observed. What's more, GSTP1 is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are thought to function in xenobiotic metabolism and play a role in susceptibility to cancer, and other diseases.

E.coli-derived human GST3 recombinant protein (Position: P2-Q210) . Human GST3 shares 85% and 86% amino acid (aa) sequences identity with mouse and rat GST3, respectively.

Cancer, Cardiovascular, Metabolism, Mitochondrial Markers, Mitochondrial Metabolism, Neurogenesis, Neurology Process, Neuroscience, Oxidative Stress, Pathways and Processes, Redox Metabolism

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration. .

1. Morrow, C. S.; Cowan, K. H.; Goldsmith, M. E. : Structure of the human genomic glutathione S-transferase-pi gene. Gene 75: 3-11, 1989. 2. Bora PS, Bora NS, Wu XL, Lange LG (Oct 1991) . Molecular cloning, sequencing, and expression of human myocardial fatty acid ethyl ester synthase-III cDNA. J Biol Chem 266 (25) : 16774–7. 3. Smith CM, Bora PS, Bora NS, Jones C, Gerhard DS (Nov 1995) . Genetic and radiation-reduced somatic cell hybrid sublocalization of the human GSTP1 gene. Cytogenet Cell Genet 71 (3) : 235–9.

Cytoplasm . Mitochondrion . Nucleus . The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization.