The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Gamma-glutamyltranspeptidase (GGT) acts as a glutathionase and catalyzes the transfer of the glutamyl moiety of glutathione to a variety of amino acids and dipeptide acceptors. This enzyme is located on the outer surface of the cell membrane and is widely distributed in mammalian tissues involved in absorption and secretion. In humans, hepatic GGT activity is elevated in some liver diseases. GGT1 is released into the bloodstream after liver damage, and an elevated level of the enzyme may be a useful early sign of hepatocellular carcinoma. GGT5 converts leukotriene C4 to leukotriene D4; it does not, however, convert synthetic substrates that are commonly used to assay GGT. In human serum and in human tissues, there is a marked heterogeneity in GGT, but this heterogeneity can be attributed to different glycosylation of the same peptide rather than to the products of different genes.
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Protein Aliases: G alpha 13; G alpha-13; G-protein subunit alpha-13; Galpha 13; Galpha13; GNA13; guanine nucleotide binding protein (G protein), alpha 13; Guanine nucleotide binding protein alpha 13 subunit; guanine nucleotide binding protein, alpha 13; Guanine nucleotide-binding protein subunit alpha-13
Gene Aliases: AU024132; AU043124; G13; Galpha13; Gna-13; GNA13