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The expression region of this recombinant Human DHFR covers amino acids 1-187. The expected molecular weight for the DHFR protein is calculated to be 25.5 kDa. This DHFR protein is produced using e.coli expression system. The DHFR gene fragment has been modified by fusing the N-terminal 6xHis tag, providing convenience in detecting and purifying the recombinant DHFR protein during the following stages.Human dihydrofolate reductase (DHFR) is a pivotal enzyme in cellular metabolism, essential for the synthesis of nucleic acids. It catalyzes the conversion of dihydrofolate to tetrahydrofolate, a vital cofactor for DNA and RNA synthesis. DHFR plays a crucial role in cell division and proliferation by ensuring an adequate supply of folate-derived cofactors for nucleotide biosynthesis. Due to its significance in cellular processes, DHFR is a target for antifolate drugs, including methotrexate, commonly used in cancer chemotherapy and autoimmune disease treatment. Understanding DHFR's function is vital for developing therapeutic strategies and elucidating folate metabolism intricacies.
The expression region of this recombinant Human DHFR covers amino acids 1-187. The expected molecular weight for the DHFR protein is calculated to be 25.5 kDa. This DHFR protein is produced using e.coli expression system. The DHFR gene fragment has been modified by fusing the N-terminal 6xHis tag, providing convenience in detecting and purifying the recombinant DHFR protein during the following stages.Human dihydrofolate reductase (DHFR) is a pivotal enzyme in cellular metabolism, essential for the synthesis of nucleic acids. It catalyzes the conversion of dihydrofolate to tetrahydrofolate, a vital cofactor for DNA and RNA synthesis. DHFR plays a crucial role in cell division and proliferation by ensuring an adequate supply of folate-derived cofactors for nucleotide biosynthesis. Due to its significance in cellular processes, DHFR is a target for antifolate drugs, including methotrexate, commonly used in cancer chemotherapy and autoimmune disease treatment. Understanding DHFR’s function is vital for developing therapeutic strategies and elucidating folate metabolism intricacies.
| Cat.No | ACP05235 | Target Name | DHFR |
|---|---|---|---|
| Target Synonyms | DHFR; DHFRP1; Dihydrofolate reductase; DYR; DYR_HUMAN; EC 1.5.1.3 | Form | Liquid or Lyophilized powder |
| Expression System | E.coli | Expression Range | 1-187aa |
| Mol Weight | 25.5 kDa | Protein Length | Full length |
| Purity | Greater than 90% as determined by SDS-PAGE. | Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P00374 |
|---|
Uniprot Id
P00374
Target Species
Human
Target Name
DHFR
Target Full Name
Dihydrofolate reductase
Target Function
Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFR2.
Target Involvement
Megaloblastic anemia due to dihydrofolate reductase deficiency (DHFRD)
Target Subcellular Location
Mitochondrion. Cytoplasm.
Target Protein Families
Dihydrofolate reductase family
Target Tissue Specificity
Widely expressed in fetal and adult tissues, including throughout the fetal and adult brains and whole blood. Expression is higher in the adult brain than in the fetal brain.
Target Research Area
Cell Biology, Signal Transduction
Target Synonyms
DHFR; DHFRP1; Dihydrofolate reductase; DYR; DYR_HUMAN; EC 1.5.1.3
Target Background
Dihydrofolate reductase converts dihydrofolate into tetrahydrofolate, a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and certain amino acids. While the functional dihydrofolate reductase gene has been mapped to chromosome 5, multiple intronless processed pseudogenes or dihydrofolate reductase-like genes have been identified on separate chromosomes. Dihydrofolate reductase deficiency has been linked to megaloblastic anemia. Several transcript variants encoding different isoforms have been found for this gene.
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