Enzymes for Research, Diagnostic and Industrial Use
Our Products Cannot Be Used As Medicines Directly For Personal Use.
Welcome! For price inquiries, please feel free to contact us through the form on the left side. We will get back to you as soon as possible.
Catalog | Product Name | EC No. | CAS No. | Source | Price |
---|---|---|---|---|---|
NATE-0857 | Matriptase-2 from Human, Recombinant | EC 3.4.21.- | Drosophila Schn... | Inquiry |
Matriptase-2, also known as TMPRSS6 (transmembrane serine protease, serine 6), is a transmembrane serine protease that plays a crucial role in iron metabolism and homeostasis. Matriptase-2 has remarkable properties and essential functions, and has attracted much attention in the field of biological and medical research.
Matriptase-2 was first recognized as a member of the type II transmembrane serine protease family in 2001. Its discovery arose from the need to understand iron metabolism and its regulation. Dysregulation of iron homeostasis has been found to lead to disorders such as hereditary hemochromatosis, which is characterized by excessive accumulation of iron. matriptase-2 is thought to play a key role in the regulation of heme, a hormone that is essential for iron absorption and storage.
Matriptase-2 consists of multiple structural domains that contribute to its function. These structural domains include a signal peptide, an extracellular structural domain containing protease activity, a transmembrane structural domain, and an intracellular cytoplasmic tail. The extracellular structural domain contains the serine protease catalytic triad that is involved in the enzymatic activity of Matriptase-2. Understanding the structure of Matriptase-2 helps to elucidate its function and interactions in the iron metabolism pathway.
Dysregulation of iron metabolism is associated with various disorders, including iron deficiency anemia and hereditary hemochromatosis. Understanding the molecular mechanisms involving Matriptase-2 presents opportunities for developing therapeutic interventions. Targeting Matriptase-2's activity or expression could help restore iron homeostasis in individuals with iron-related disorders.
Monitoring Matriptase-2 levels has emerged as a potential biomarker for diagnosing and monitoring iron-related diseases. Studies have identified alterations in Matriptase-2 expression and activity in patients with conditions like hereditary hemochromatosis and iron deficiency anemia. Utilizing Matriptase-2 as a diagnostic tool may provide valuable insights into disease progression and treatment response.
Matriptase-2 mutations have been implicated in hereditary hemochromatosis, a condition characterized by excessive iron absorption. Understanding the role of Matriptase-2 in iron regulation provides insights into the pathogenesis of this disorder, potentially leading to novel therapeutic strategies.
Matriptase-2's involvement in hepcidin regulation makes it a potential target for treating anemia, particularly iron deficiency anemia. By modulating hepcidin expression and iron availability, therapies targeting Matriptase-2 may enhance iron absorption and red blood cell production in individuals with anemia.
Future studies of Matriptase-2 may focus on unraveling its complex regulatory mechanisms and identifying its potential interactions with other proteins involved in iron metabolism. In addition, studying the potential therapeutic applications of modulating Matriptase-2 activity offers hope for patients with iron-related diseases. Understanding the complex role of Matriptase-2 in iron homeostasis will help improve diagnostic and therapeutic strategies for anemia, hereditary hemochromatosis, and other iron-related diseases.