Recombinant Human GGT5, N-His

Reference: YHE17101
Product nameRecombinant Human GGT5, N-His
Uniprot IDP36269
Origin speciesHomo sapiens (Human)
Expression systemProcaryotic expression
Protein delivered with Tag?N-Terminal His Tag
Buffer0.01M PBS, pH 7.4.
Delivery conditionDry Ice
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
Host speciesEscherichia coli (E.coli)
Aliases /SynonymsGGTLA1, Gamma-glutamyl transpeptidase-related enzyme, Gamma-glutamyltranspeptidase 5, Glutathione hydrolase 5 proenzyme, GGT 5, Gamma-glutamyltransferase 5, GGT5, Leukotriene-C4 hydrolase, Gamma-glutamyltransferase-like activity 1, GGT-rel
NoteFor research use only

Description of Recombinant Human GGT5, N-His


Recombinant Human GGT5, N-His is a protein that plays a crucial role in various biological processes. It is a drug target that has been extensively studied due to its potential therapeutic applications. In this article, we will discuss the structure, activity, and applications of this protein in detail.

Structure of Recombinant Human GGT5, N-His

Recombinant Human GGT5, N-His is a member of the gamma-glutamyltransferase (GGT) family of enzymes. It is a type II transmembrane protein that is composed of 583 amino acids. The protein has a molecular weight of approximately 65 kDa and is composed of two subunits – a heavy subunit of 50 kDa and a light subunit of 22 kDa. The heavy subunit contains the active site of the enzyme, while the light subunit is responsible for anchoring the protein to the cell membrane.

The crystal structure of Recombinant Human GGT5, N-His has been determined, revealing a unique conformation of the active site. The protein contains a large cavity that accommodates the substrate and a catalytic triad consisting of cysteine, glutamate, and histidine residues. This triad is essential for the enzymatic activity of GGT5.

Activity of this protein

Recombinant Human GGT5, N-His is primarily involved in the metabolism of glutathione, an important antioxidant molecule. It catalyzes the transfer of the gamma-glutamyl group from glutathione to an acceptor molecule, producing cysteinylglycine and a gamma-glutamyl-amino acid. This process is crucial for maintaining the balance of glutathione levels in the cell, which is essential for cellular redox homeostasis.

Apart from its role in glutathione metabolism, Recombinant Human GGT5, N-His has been shown to have other functions as well. It has been reported to play a role in the development and progression of cancer, as well as in drug resistance. Studies have also suggested that GGT5 may have a role in regulating immune responses and inflammation.

Application of Recombinant Human GGT5, N-His

Recombinant Human GGT5, N-His has emerged as a potential drug target due to its involvement in various disease processes. Inhibitors of GGT5 have been developed and tested for their potential as anticancer agents. These inhibitors have shown promising results in preclinical studies, and clinical trials are currently underway to evaluate their efficacy in cancer treatment.

Moreover, Recombinant Human GGT5, N-His inhibitors have also been investigated for their potential in the treatment of drug-resistant cancers. GGT5 has been found to be upregulated in many drug-resistant cancer cells, making it an attractive target for overcoming drug resistance.

In addition to cancer, Recombinant Human GGT5, N-His has also been implicated in other diseases, such as liver diseases and neurodegenerative disorders. Studies have shown that GGT5 levels are elevated in patients with liver diseases, and targeting this protein may have therapeutic benefits. Furthermore, GGT5 has been found to be involved in the production of reactive oxygen species, which are implicated in the pathogenesis of neurodegenerative disorders. Therefore, targeting GGT5 may also have potential in the treatment of these diseases.


In conclusion, Recombinant Human GGT5, N-His is a crucial protein with diverse functions and potential therapeutic applications. Its unique structure and enzymatic activity make it an attractive drug target for various diseases, particularly cancer. Further research in this field may lead to the development of novel treatments for a wide range of diseases.


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