|Application ||WB, E|
|Other Accession||NP_005256.2, 2678|
|Calculated MW||61410 Da|
|Other Names||Gamma-glutamyltranspeptidase 1, GGT 1, 22.214.171.124, Gamma-glutamyltransferase 1, Glutathione hydrolase 1, 126.96.36.199, Leukotriene-C4 hydrolase, 188.8.131.52, CD224, Gamma-glutamyltranspeptidase 1 heavy chain, Gamma-glutamyltranspeptidase 1 light chain, GGT1, GGT|
|Format||0.5 mg/ml in Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||GGT1 Antibody (internal region, near N-Term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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.|
|Cellular Location||Cell membrane; Single-pass type II membrane protein|
|Tissue Location||Detected in fetal and adult kidney and liver, adult pancreas, stomach, intestine, placenta and lung. Isoform 3 is lung-specific. There are several other tissue-specific forms that arise from alternative promoter usage but that produce the same protein|
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Provided below are standard protocols that you may find useful for product applications.
Reported variants represent identical protein: NP_038347.2, NP_001027536.1, NP_001027537.1, NP_005256.2.
Autocatalytic cleavage of human gamma-glutamyl transpeptidase is highly dependent on N-glycosylation at asparagine 95. West MB, Wickham S, Quinalty LM, Pavlovicz RE, Li C, Hanigan MH. J Biol Chem. 2011 Aug 19;286(33):28876-88. PMID: 21712391
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