GGT1 polyclonal, anti-human
€470.00
In stock
SKU
AC-AP73449
Background:
Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.
Other Names:
GGT1; GGT; Gamma-glutamyltranspeptidase 1; GGT 1; Gamma-glutamyltransferase 1; Glutathione hydrolase 1; Leukotriene-C4 hydrolase; CD224
Antigen Type: synthetic peptide
Antigen Type: GGT1
Gene ID: 2678
Primary Accession: P19440
Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.
Other Names:
GGT1; GGT; Gamma-glutamyltranspeptidase 1; GGT 1; Gamma-glutamyltransferase 1; Glutathione hydrolase 1; Leukotriene-C4 hydrolase; CD224
Antigen Type: synthetic peptide
Antigen Type: GGT1
Gene ID: 2678
Primary Accession: P19440
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