GGT1 Protein, Human (HEK293, His)

The GGT1 protein cleaves gamma-glutamyl bonds of extracellular glutathione, glutathione conjugates, and other gamma-glutamyl compounds. Its metabolism releases free glutamate and cysteinylglycine, which are hydrolyzed into cysteine and glycine. GGT1 Protein, Human (HEK293, His) is the recombinant human-derived GGT1 protein, expressed by HEK293 , with N-His labeled tag.

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.

The enzyme activity of this recombinant protein is testing in progress, we cannot offer a guarantee yet.

Human

HEK293

N-8*His

P19440-1 (P27-Y569)

2678  [NCBI]

Extracellular Domain

PSASKEPDNHVYTRAAVAADAKQCSKIGRDALRDGGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEVINAREVAPRLAFATMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAALENKRTVIEQQPVLCEVFCRDRKVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKDIQAAGGIVTAEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFSRESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRAQISDDTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNEMDDFSSPSITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTATALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAASDSRKGGEPAGY

Approximately 55-65 kDa (heavy chain) & 25-30 kDa (light chain),based on SDS-PAGE under reducing conditions,due to the glycosylation.

≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4. Normally 8% trehalose is added as protectant before lyophilization.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.