Recombinant Human GGT1 His-tag Protein, CF

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Gamma-glutamyl transferase 1 (GGT1), also known as Gamma-glutamyl transpeptidase 1, is a ubiquitous enzyme that cleaves the gamma-glutamyl bond substrates where the glutamate moiety is available. This makes GGT1 crucial for metabolism of glutathione, the most important cellular antioxidant in humans and for its role in leukotriene biosynthesis, required for lipid metabolism. Although GGT1 comes from a 7 member multigene family, only GGT1 and GGT5 have enzymatic activity (1, 2). GGT5 has 40% amino acid homology with GGT1 and only 4% of the activity (2, 3) making GGT1 the primary contributor to enzymatic activity in the cells. GGT1 is synthesized as a single 569 amino acid polypeptide that is autocleaved by threonine 381 into a mature, activated, heterodimeric glycoprotein composed of a large subunit with an N-terminal hydrophobic transmembrane domain that anchors the enzyme to the membrane and a small catalytic subunit containing the catalytic nucleophile threonine 381 (4, 5). The human GGT1 active site is located in a deep channel but remains in an open configuration (4). It has a unique buried chloride ion that is integral to the protein structure (4). GGT1 contributes to cysteine homeostasis, intracellular redox, and inflammation (2, 6-8) and has been implicated to play a role in Parkinson and cardiovascular disease (5, 9), is a diagnostic marker of several diseases including liver and pancreatic cancer and is induced in several cancers to contribute to resistance to chemotherapeutic agents (7, 10-14). 

Array 10977-GT

• GGT1 Antibodies
• GGT1 ELISA Kits
• GGT1 Lysates
• GGT1 Proteins and Enzyme