Recombinant Human GLO1 Protein, N-His

Description of Recombinant Human GLO1 Protein, N-His

Introduction

Recombinant proteins are proteins that are produced through genetic engineering techniques, where the DNA sequence of the desired protein is inserted into an expression vector and then expressed in a host organism. This allows for the production of large quantities of a specific protein, which can be used for various purposes, including research, diagnostics, and therapeutics. One such recombinant protein is the human GLO1 protein, which has significant implications in the field of biochemistry and medicine.

Structure of Recombinant Human GLO1 Protein

The human GLO1 protein, also known as glyoxalase I, is an enzyme that plays a crucial role in cellular detoxification by catalyzing the conversion of toxic methylglyoxal (MG) into D-lactate. The gene encoding this protein is located on chromosome 6 and consists of 12 exons. The recombinant human GLO1 protein is composed of 184 amino acids and has a molecular weight of approximately 21 kDa. It has a highly conserved structure, with 92% sequence identity among different species, indicating its essential role in cellular function.

The crystal structure of the recombinant human GLO1 protein has been determined, revealing a homodimeric structure with each monomer containing a catalytic site. The active site of the enzyme consists of a zinc ion, which is essential for its catalytic activity. The dimeric structure of the protein allows for efficient binding and processing of MG, making it an efficient detoxifying enzyme.

Activity of Recombinant Human GLO1 Protein

The primary function of the recombinant human GLO1 protein is to detoxify the cell by converting MG into D-lactate. MG is a reactive carbonyl compound that is produced as a byproduct of cellular metabolism and can cause damage to cellular components, including proteins, DNA, and lipids. The accumulation of MG has been linked to various diseases, such as diabetes, neurodegenerative disorders, and cancer. The recombinant human GLO1 protein plays a crucial role in preventing the harmful effects of MG by maintaining its levels within the cell.

In addition to its role in detoxification, the recombinant human GLO1 protein has been shown to have other functions, such as regulating cell growth and apoptosis. It has been reported that GLO1 deficiency leads to increased cell proliferation and resistance to apoptosis, which can contribute to the development of cancer. Furthermore, the enzyme has been found to have anti-inflammatory properties and can protect against oxidative stress, making it a potential therapeutic target for various diseases.

Application of Recombinant Human GLO1 Protein

The recombinant human GLO1 protein has various applications in the field of research, diagnostics, and therapeutics. Its ability to detoxify the cell makes it a valuable tool for studying the role of MG in different diseases. It can also be used for the development of diagnostic assays to measure MG levels in biological samples, providing insights into the progression of diseases such as diabetes and cancer.

Moreover, the recombinant human GLO1 protein has potential therapeutic applications. As mentioned earlier, its deficiency has been linked to various diseases, and its overexpression has been shown to have anti-cancer effects. Therefore, the enzyme can be used as a potential target for drug development to treat diseases associated with MG accumulation.

Conclusion

In summary, the recombinant human GLO1 protein is a crucial enzyme involved in cellular detoxification and has significant implications in various diseases. Its structure, activity, and applications make it a valuable tool for research and a potential therapeutic target. Further studies and developments in this field can provide a better understanding of the role of this enzyme in health and disease.