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100µg
Homo sapiens (Human)
AntibodySystem
AntibodySystem, Recombinant Proteins
Escherichia coli (E. coli)
Procaryotic expression
Recombinant Human GLS, N-His is a protein that plays a crucial role in cellular metabolism and is a potential drug target for various diseases. This protein is a recombinant form of human glutaminase (GLS) that has been genetically modified to contain a histidine (His) tag at the N-terminus. The addition of this tag allows for easy purification and detection of the protein, making it a valuable tool for research and potential therapeutic applications.
The structure of Recombinant Human GLS, N-His is composed of two subunits, GLS1 and GLS2, which are encoded by the GLS gene. These subunits come together to form a homodimeric protein with a molecular weight of approximately 73 kDa. Each subunit contains a catalytic domain at the C-terminus and a regulatory domain at the N-terminus. The addition of the N-His tag does not alter the overall structure of the protein, making it a reliable model for studying the function of GLS in various cellular processes.
Recombinant Human GLS, N-His is a key enzyme in the process of glutaminolysis, which is the conversion of glutamine to glutamate and ammonia. This process plays a critical role in cellular metabolism, providing energy and building blocks for various biosynthetic pathways. GLS is also involved in the regulation of cellular redox balance and the synthesis of key molecules such as glutathione and nucleotides. The addition of the N-His tag does not affect the activity of GLS, allowing for accurate analysis of its enzymatic function.
The potential therapeutic applications of Recombinant Human GLS, N-His are vast and diverse. As a drug target, GLS has been implicated in various diseases such as cancer, neurodegenerative disorders, and metabolic disorders. In cancer, GLS plays a critical role in providing energy and building blocks for tumor growth, making it an attractive target for anti-cancer therapies. In neurodegenerative disorders such as Alzheimer’s disease, GLS has been shown to be dysregulated, leading to impaired glutamate signaling and neuronal damage. Therapies targeting GLS could potentially mitigate these effects and slow the progression of the disease.
Furthermore, Recombinant Human GLS, N-His has been used as a research tool in various studies investigating the role of GLS in cellular metabolism and disease. The N-His tag allows for easy purification of the protein, making it a valuable tool for studying its structure and function. It has also been used in drug discovery efforts to screen for potential inhibitors of GLS, which could lead to the development of novel therapies.
In conclusion, Recombinant Human GLS, N-His is a valuable protein with a wide range of applications in both research and potential therapeutic interventions. Its structure and activity make it an ideal model for studying the role of GLS in cellular metabolism and disease. With its potential as a drug target, this protein holds promise for the development of new and effective treatments for various diseases.
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