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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human MTHFD1 Protein, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 34.34 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
Brand | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | Met1-Lys297 |
Aliases /Synonyms | MTHFC, C1-THF synthase, MTHFD1, C-1-tetrahydrofolate synthase, cytoplasmic, MTHFD |
Reference | ARO-P12278 |
Note | For research use only. |
Recombinant Human MTHFD1 Protein, also known as Methylenetetrahydrofolate dehydrogenase 1, is a key enzyme involved in the folate metabolism pathway. It is a highly conserved protein found in all organisms, from bacteria to humans. This protein has been extensively studied due to its crucial role in maintaining the balance of folate and homocysteine levels in the body. In this article, we will discuss the structure, activity, and applications of Recombinant Human MTHFD1 Protein in detail.
The gene encoding MTHFD1 is located on chromosome 14 in humans and consists of 22 exons. The protein is composed of 1051 amino acids with a molecular weight of approximately 117 kDa. It has a highly conserved N-terminal region containing a nucleotide-binding domain, a central catalytic domain, and a C-terminal regulatory domain. The catalytic domain is responsible for the enzyme’s activity, while the regulatory domain modulates its function.
Recombinant Human MTHFD1 Protein is produced using recombinant DNA technology in a variety of expression systems, including E. coli, yeast, and insect cells. The protein is purified using various chromatographic techniques, resulting in a highly pure and active form of the enzyme.
MTHFD1 is a trifunctional enzyme that catalyzes three consecutive reactions in the folate metabolism pathway. It converts 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate, which is then converted to 10-formyltetrahydrofolate. This form of folate is essential for the synthesis of purines and thymidylate, which are crucial for DNA replication and cell growth.
In addition to its role in folate metabolism, MTHFD1 also plays a critical role in the regulation of homocysteine levels. It converts homocysteine to methionine, an essential amino acid, in a process called remethylation. This process prevents the accumulation of homocysteine, which can be toxic to cells and is associated with various diseases, including cardiovascular disease and neural tube defects.
Recombinant Human MTHFD1 Protein has been shown to have similar activity to the native enzyme, making it a valuable tool for studying the role of MTHFD1 in various biological processes. It has also been used in enzyme replacement therapy for individuals with MTHFD1 deficiency, a rare genetic disorder that affects the enzyme’s activity and can lead to severe health complications.
Recombinant Human MTHFD1 Protein has a wide range of applications in both research and clinical settings. Its role in folate metabolism and homocysteine regulation makes it a valuable tool for studying the mechanisms of various diseases, including cancer, cardiovascular disease, and neural tube defects. It is also used in the development of diagnostic tests for MTHFD1 deficiency and other disorders related to folate metabolism.
In addition to its research applications, Recombinant Human MTHFD1 Protein has potential therapeutic applications. As mentioned earlier, it has been used in enzyme replacement therapy for individuals with MTHFD1 deficiency. It has also shown promise in the treatment of certain types of cancer, as targeting MTHFD1 can disrupt the production of purines and thymidylate, which are essential for cancer cell growth.
In conclusion, Recombinant Human MTHFD1 Protein is a crucial enzyme involved in the folate metabolism pathway and the regulation of homocysteine levels. Its structure and activity have been extensively studied, and it has various applications
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