GGT1 Protein, Human (HEK293, His)

GGT1 Protein cleaves the gamma-glutamyl bond of extracellular glutathione, glutathione conjugates, and other gamma-glutamyl compounds. Its metabolism releases free glutamate and cysteinyl-glycine, hydrolyzed to cysteine and glycine. In the presence of high dipeptide concentrations, it catalyzes transpeptidation, forming new gamma-glutamyl compounds. GGT1 contributes to cysteine and glutathione homeostasis and converts leukotriene LTC4 to LTD4. Note: GGT1 seems to be inactive. GGT1 Protein, Human (HEK293, His) is the recombinant human-derived GGT1 protein, expressed by HEK293, with N-His labeled tag. The total length of GGT1 Protein, Human (HEK293, His) is 543 a.a., with molecular weight of 55-65 kDa (heavy chain) & 25-30 kDa (light chain), respectively.

The GGT1 protein plays a pivotal role in cellular metabolism by cleaving the gamma-glutamyl bond in various substrates, including extracellular glutathione, glutathione conjugates such as maresin conjugate (13R)-S-glutathionyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate (MCTR1), and other gamma-glutamyl compounds like leukotriene C4 (LTC4). This enzymatic activity results in the release of free glutamate and the dipeptide cysteinyl-glycine, which can be further hydrolyzed to cysteine and glycine by dipeptidases. Under conditions of elevated dipeptides and certain amino acids, GGT1 can catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid and forming a new gamma-glutamyl compound. Beyond its involvement in cysteine and glutathione homeostasis, GGT1 contributes to the conversion of leukotriene LTC4 to LTD4. It is noteworthy that GGT1 appears to be inactive under certain circumstances.

Human

HEK293

N-His

P19440-1 (P27-Y569)

2678  [NCBI]

55-65 kDa (heavy chain) & 25-30 kDa (light chain)

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.