GGT1 (aa180-193) Antibody (internal region)
Peptide-affinity purified goat antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
---|---|
Primary Accession | P19440 |
Other Accession | NP_005256.2, 2678 |
Reactivity | Human |
Host | Goat |
Clonality | Polyclonal |
Concentration | 0.5 mg/ml |
Isotype | IgG |
Calculated MW | 61410 Da |
Gene ID | 2678 |
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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 |
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 (aa180-193) Antibody (internal region) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | GGT1 |
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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:21447318, PubMed:7673200, PubMed:7759490, PubMed:8095045, PubMed:8827453). 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 |
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Provided below are standard protocols that you may find useful for product applications.
Background
Reported variants represent identical protein: NP_038347.2, NP_001027536.1, NP_001027537.1, NP_005256.2.
References
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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