Recombinant Mouse TGM2 Protein, N-His

Description of Recombinant Mouse TGM2 Protein, N-His

Introduction

Recombinant Mouse TGM2 Protein, also known as Transglutaminase 2, is a highly conserved enzyme that plays a crucial role in various biological processes. This protein is expressed in different tissues and has been extensively studied for its structure, activity, and applications in various fields of research. In this article, we will provide a scientific description of Recombinant Mouse TGM2 Protein, highlighting its structure, activity, and applications.

Structure of Recombinant Mouse TGM2 Protein

Recombinant Mouse TGM2 Protein is a 78 kDa protein consisting of 687 amino acids. It is a member of the transglutaminase family, which is characterized by a highly conserved catalytic domain and a C-terminal domain responsible for substrate recognition and binding. The catalytic domain of TGM2 contains the active site cysteine residue, which is essential for its enzymatic activity. The C-terminal domain of TGM2 contains several ankyrin repeats, which are involved in protein-protein interactions and play a role in regulating the activity of the enzyme.

Recombinant Mouse TGM2 Protein also contains two Ca2+-binding sites, which are essential for its activity. The binding of Ca2+ ions induces a conformational change in the protein, exposing the active site and allowing it to interact with its substrates. This conformational change is crucial for the catalytic activity of TGM2.

Activity of Recombinant Mouse TGM2 Protein

Recombinant Mouse TGM2 Protein is a multifunctional enzyme with both transamidating and GTPase activities. Its transamidating activity involves the formation of covalent bonds between the γ-carboxamide group of a glutamine residue and the ε-amino group of a lysine residue in a protein or peptide substrate. This activity is responsible for the cross-linking of proteins, which is important for the stability and function of various tissues and organs.

The GTPase activity of TGM2 is involved in the regulation of its transamidating activity. It hydrolyzes GTP to GDP, which leads to the inactivation of the enzyme. This activity is regulated by various factors, including Ca2+ ions and the redox state of the cell. In addition, TGM2 can also act as a protein disulfide isomerase, which is important for the correct folding of proteins.

Applications of Recombinant Mouse TGM2 Protein

Recombinant Mouse TGM2 Protein has a wide range of applications in various fields of research. Its transamidating activity has been extensively studied in the context of tissue repair and wound healing. TGM2 is involved in the formation of a fibrin clot, which is essential for wound healing. In addition, it plays a role in the regulation of cell adhesion and migration, which are important processes in tissue repair.

Furthermore, the transamidating activity of TGM2 has been linked to various diseases, including neurodegenerative disorders, celiac disease, and cancer. In neurodegenerative disorders, TGM2 has been shown to contribute to the formation of protein aggregates, which are a hallmark of these diseases. In celiac disease, TGM2 is involved in the immune response to gluten, leading to tissue damage in the small intestine. In cancer, TGM2 has been shown to promote cell survival and metastasis, making it a potential therapeutic target for cancer treatment.

Moreover, Recombinant Mouse TGM2 Protein has been used in various biotechnological applications, such as protein engineering and drug discovery. Its transamidating activity has been utilized to create protein conjugates with improved stability and activity, as well as to develop new methods for drug delivery. In addition, TGM2 has been used as a target for drug screening, leading to the identification of potential inhibitors with therapeutic