Recombinant Mouse QSOX1 Protein, N-His

Description of Recombinant Mouse QSOX1 Protein, N-His

Introduction

Recombinant Mouse QSOX1 Protein, also known as Quiescin Sulfhydryl Oxidase 1, is a highly conserved enzyme that plays a crucial role in protein folding and disulfide bond formation. It is a member of the QSOX family of enzymes, which are found in all eukaryotic organisms and are involved in the oxidative folding of proteins. In this article, we will discuss the structure, activity, and applications of Recombinant Mouse QSOX1 Protein.

Structure of Recombinant Mouse QSOX1 Protein

Recombinant Mouse QSOX1 Protein is a homodimeric enzyme, meaning it is composed of two identical subunits. Each subunit contains two distinct domains: a thioredoxin-like domain and a flavin adenine dinucleotide (FAD)-binding domain. The thioredoxin-like domain is responsible for the catalytic activity of the enzyme, while the FAD-binding domain is involved in the redox reactions of the enzyme.

The crystal structure of Recombinant Mouse QSOX1 Protein has been determined, revealing the detailed arrangement of the two subunits and their active sites. The enzyme has a compact globular structure, with the active site located at the interface of the two subunits. The active site contains a highly conserved CXXC motif, which is responsible for the catalytic activity of the enzyme.

Activity of Recombinant Mouse QSOX1 Protein

Recombinant Mouse QSOX1 Protein has two main activities: sulfhydryl oxidase and disulfide bond formation. As a sulfhydryl oxidase, the enzyme catalyzes the oxidation of free thiols (sulfhydryl groups) to form disulfide bonds. This process is essential for the correct folding and stability of many proteins. Recombinant Mouse QSOX1 Protein has been shown to have a broad substrate specificity, oxidizing a wide range of proteins with different structures and functions.

In addition to its sulfhydryl oxidase activity, Recombinant Mouse QSOX1 Protein also has disulfide bond formation activity. This involves the transfer of electrons from reduced glutathione (GSH) to the newly formed disulfide bonds, resulting in the formation of oxidized glutathione (GSSG). This redox reaction is important for maintaining the redox balance in the cell and is crucial for the proper functioning of various cellular processes.

Applications of Recombinant Mouse QSOX1 Protein

Recombinant Mouse QSOX1 Protein has various applications in both basic research and biotechnology. Its ability to catalyze the formation of disulfide bonds makes it a valuable tool for studying protein folding and structure. It has been used in in vitro studies to investigate the folding and stability of various proteins, including antibodies, enzymes, and growth factors.

In biotechnology, Recombinant Mouse QSOX1 Protein is used in the production of recombinant proteins. Many proteins require disulfide bonds for their proper folding and activity, and the addition of Recombinant Mouse QSOX1 Protein to the production process can improve the yield and quality of these proteins. This is particularly important for the production of therapeutic proteins, such as antibodies and enzymes, which are used in the treatment of various diseases.

Furthermore, Recombinant Mouse QSOX1 Protein has potential applications in the food industry. It has been shown to improve the texture and shelf life of food products by promoting the formation of disulfide bonds in proteins, which can increase their stability and resistance to heat and mechanical stress.

Conclusion

In summary, Recombinant Mouse QSOX1 Protein is a highly conserved enzyme with a homodimeric structure and two main activities: sulfhydryl oxidase and disulfide bond formation. Its broad substrate specificity and ability to catalyze the formation of disulfide bonds make it a valuable tool in protein folding studies and recom