Recombinant Mouse CD26/DPP4 Protein, N-His

Description of Recombinant Mouse CD26/DPP4 Protein, N-His

Introduction to Recombinant Mouse CD26/DPP4 Protein

Recombinant Mouse CD26/DPP4 Protein, also known as dipeptidyl peptidase-4 (DPP4), is a type II transmembrane glycoprotein that is expressed on the surface of various cell types, including T cells, B cells, natural killer cells, and epithelial cells. It is a member of the prolyl oligopeptidase family and plays a crucial role in regulating immune responses and glucose metabolism.

Structure of Recombinant Mouse CD26/DPP4 Protein

The primary structure of Recombinant Mouse CD26/DPP4 Protein consists of 766 amino acids, with a predicted molecular weight of approximately 88 kDa. It is composed of an extracellular domain, a transmembrane domain, and a cytoplasmic domain. The extracellular domain contains a cysteine-rich region, a glycosylation site, and the active site for enzymatic activity. The transmembrane domain anchors the protein to the cell membrane, while the cytoplasmic domain is involved in intracellular signaling.

The crystal structure of Recombinant Mouse CD26/DPP4 Protein has been determined, revealing a homodimeric protein with a characteristic butterfly-shaped structure. Each monomer consists of an N-terminal β-propeller domain and a C-terminal α/β-hydrolase domain. The β-propeller domain is responsible for substrate binding, while the α/β-hydrolase domain contains the catalytic site for enzymatic activity.

Enzymatic Activity of Recombinant Mouse CD26/DPP4 Protein

Recombinant Mouse CD26/DPP4 Protein is a serine protease that cleaves dipeptides from the N-terminus of polypeptides. It specifically cleaves dipeptides with proline or alanine at the penultimate position, hence the name prolyl oligopeptidase. This enzymatic activity is essential for the regulation of various physiological processes, including immune responses, glucose metabolism, and cell signaling.

One of the main substrates of Recombinant Mouse CD26/DPP4 Protein is the incretin hormone glucagon-like peptide-1 (GLP-1). DPP4 cleaves the N-terminal dipeptide from GLP-1, inactivating its insulinotropic and anorectic effects. This process plays a crucial role in glucose homeostasis and is a target for the treatment of type 2 diabetes.

In addition to GLP-1, Recombinant Mouse CD26/DPP4 Protein also cleaves other peptides involved in immune responses, such as neuropeptide Y and substance P. This activity has been linked to the regulation of inflammation and autoimmune diseases.

Applications of Recombinant Mouse CD26/DPP4 Protein

Recombinant Mouse CD26/DPP4 Protein has a wide range of applications in both research and clinical settings. Its enzymatic activity and role in immune regulation make it a valuable tool in studying various diseases, including diabetes, cancer, and autoimmune disorders.

In research, Recombinant Mouse CD26/DPP4 Protein is commonly used to study the role of DPP4 in different physiological processes. It can also be used to screen for potential DPP4 inhibitors, which have therapeutic potential in the treatment of diabetes and other diseases.

In the clinical setting, Recombinant Mouse CD26/DPP4 Protein is used as a diagnostic marker for certain diseases, such as pancreatic cancer and rheumatoid arthritis. DPP4 levels in the blood have been shown to correlate with disease severity and progression, making it a potential biomarker for these conditions.

Conclusion

In summary, Recombinant Mouse CD26/DPP4 Protein is a multifunctional protein with a crucial role in regulating immune responses and glucose metabolism. Its structure, enzym