Recombinant Human GSTT2, N-His

Description of Recombinant Human GSTT2, N-His

Introduction

Recombinant Human GSTT2, N-His is a protein that has been genetically engineered for use in research and drug development. It belongs to the glutathione S-transferase (GST) family of enzymes, which play a crucial role in the detoxification of xenobiotics and endogenous compounds in the body.

Structure of Recombinant Human GSTT2, N-His

The protein is composed of 217 amino acids with a molecular weight of approximately 25 kDa. It contains a histidine tag at the N-terminus, which allows for easy purification and detection. The crystal structure of Recombinant Human GSTT2, N-His has been determined, revealing a dimeric structure with each monomer consisting of two domains: the N-terminal domain and the C-terminal domain.

The N-terminal domain contains the active site, which is responsible for the catalytic activity of the enzyme. It consists of a conserved glutathione binding site and a hydrophobic substrate binding site. The C-terminal domain, on the other hand, is involved in protein-protein interactions and is responsible for the dimerization of the enzyme.

Activity of this protein

Recombinant Human GSTT2, N-His exhibits glutathione-dependent activity, which is characteristic of all GST enzymes. It catalyzes the conjugation of glutathione (GSH) with various electrophilic compounds, resulting in the formation of a less toxic and more water-soluble product. This detoxification process is essential for protecting cells from oxidative stress and maintaining cellular homeostasis.

The enzyme has a broad substrate specificity, allowing it to detoxify a wide range of compounds, including environmental toxins, drugs, and endogenous metabolites. Some of the substrates of Recombinant Human GSTT2, N-His include benzene, ethylene oxide, and aflatoxin B1.

Application of Recombinant Human GSTT2, N-His

Due to its role in detoxification, Recombinant Human GSTT2, N-His has been identified as a potential drug target for the treatment of various diseases. Studies have shown that altered levels of GST enzymes, including GSTT2, are associated with increased susceptibility to certain diseases, such as cancer, neurodegenerative disorders, and asthma.

In addition to its therapeutic potential, Recombinant Human GSTT2, N-His is also widely used in research as a tool to study the role of GST enzymes in drug metabolism, toxicology, and disease. The histidine tag present in the protein allows for easy purification and detection, making it a valuable tool for protein-protein interaction studies and drug screening assays.

Conclusion

Recombinant Human GSTT2, N-His is a genetically engineered protein with a well-defined structure and glutathione-dependent activity. Its broad substrate specificity and potential as a drug target make it a promising candidate for therapeutic interventions. Furthermore, its use as a research tool has contributed to a better understanding of the role of GST enzymes in various biological processes. As research in this field continues, Recombinant Human GSTT2, N-His is expected to play a significant role in drug development and disease management.