GGT1 / GGT Antibody (aa1-226)
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P |
---|---|
Primary Accession | P19440 |
Reactivity | Human, Mouse |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 61kDa |
Dilution | IHC-P (10 µg/ml), WB (1:500-1:3000), |
Gene ID | 2678 |
---|---|
Other Names | Gamma-glutamyltranspeptidase 1, GGT 1, 2.3.2.2, Gamma-glutamyltransferase 1, Glutathione hydrolase 1, 3.4.19.13, Leukotriene-C4 hydrolase, 3.4.19.14, CD224, Gamma-glutamyltranspeptidase 1 heavy chain, Gamma-glutamyltranspeptidase 1 light chain, GGT1, GGT |
Target/Specificity | Human GGT1 / GGT |
Reconstitution & Storage | Keep as concentrated solution. Aliquot and store at -20°C or below. Avoid multiple freeze-thaw cycles. |
Precautions | GGT1 / GGT Antibody (aa1-226) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | GGT1 |
---|---|
Synonyms | GGT |
Function | Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates (such as maresin conjugate (13R)-S-glutathionyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)- docosahexaenoate, MCTR1) and other gamma-glutamyl compounds (such as leukotriene C4, LTC4) (PubMed:17924658, PubMed:21447318, PubMed:27791009). The metabolism of glutathione by GGT1 releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases (PubMed:27791009). 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 (PubMed:17924658, PubMed:7673200, PubMed:7759490, PubMed:8095045, PubMed:8827453, PubMed:21447318). Contributes to cysteine homeostasis, glutathione homeostasis and in the conversion of the leukotriene LTC4 to LTD4. |
Cellular Location | Cell membrane; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P07314} |
Tissue Location | Detected in fetal and adult kidney and liver, adult pancreas, stomach, intestine, placenta and lung. There are several other tissue-specific forms that arise from alternative promoter usage but that produce the same protein |
Volume | 50 µl |
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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.
References
Rajpert-De Meyts E.,et al.Proc. Natl. Acad. Sci. U.S.A. 85:8840-8844(1988).
Sakamuro D.,et al.Gene 73:1-9(1988).
Pitot H.C.,et al.Toxicol. Appl. Pharmacol. 97:23-34(1989).
Goodspeed D.C.,et al.Gene 76:1-9(1989).
Pawlak A.,et al.J. Biol. Chem. 265:3256-3262(1990).
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