Specification
| Description | Recombinant protein from the full-length sequence of Homo sapiens mitochondrial amidoxime reducing component 1 (MTARC1) (NM_022746). |
| Organism | Homo sapiens (Human) |
| Expression Host | Human Cells |
| Tag Info | His or DYKDDDDK. Please contact us if you need further information or require specific designed tag. |
| Purity | Greater than 90% by SDS-PAGE gel |
| Uniprot ID | Q5VT66 |
| Entry Name | MARC1_HUMAN |
| Gene Names | MTARC1 MARC1 MOSC1 |
| Alternative Gene Names | MARC1 MOSC1 |
| Alternative Protein Names | Mitochondrial amidoxime-reducing component 1 (mARC1) (EC 1.7.-.-) (Molybdenum cofactor sulfurase C-terminal domain-containing protein 1) (MOSC domain-containing protein 1) (Moco sulfurase C-terminal domain-containing protein 1) |
| Application | Antigens, Western, ELISA and other in vitro binding or in vivo functional assays, and protein-protein interaction studies; For research & development use only! |
| Buffer | Purified protein formulated in a sterile solution of PBS buffer, pH7.2, without any preservatives |
| Endotoxin | Endotoxin level is < 0.1 ng/µg of protein (<1EU /µg) |
| Length | 337 |
| Molecular Weight(Da) | 37499 |
| Protein Sequence | (The sequence of expressed protein may have some variation from the sequence shown below. Please contact us for the exact sequence.) MGAAGSSALARFVLLAQSRPGWLGVAALGLTAVALGAVAWRRAWPTRRRRLLQQVGTVAQLWIYPVKSCKGVPVSEAECTAMGLRSGNLRDRFWLVINQEGNMVTARQEPRLVLISLTCDGDTLTLSAAYTKDLLLPIKTPTTNAVHKCRVHGLEIEGRDCGEATAQWITSFLKSQPYRLVHFEPHMRPRRPHQIADLFRPKDQIAYSDTSPFLILSEASLADLNSRLEKKVKATNFRPNIVISGCDVYAEDSWDELLIGDVELKRVMACSRCILTTVDPDTGVMSRKEPLETLKSYRQCDPSERKLYGKSPLFGQYFVLENPGTIKVGDPVYLLGQ |
Background
| Function | FUNCTION: Catalyzes the reduction of N-oxygenated molecules, acting as a counterpart of cytochrome P450 and flavin-containing monooxygenases in metabolic cycles (PubMed:19053771, PubMed:21029045, PubMed:30397129). As a component of prodrug-converting system, reduces a multitude of N-hydroxylated prodrugs particularly amidoximes, leading to increased drug bioavailability (PubMed:19053771). May be involved in mitochondrial N(omega)-hydroxy-L-arginine (NOHA) reduction, regulating endogenous nitric oxide levels and biosynthesis (PubMed:21029045). Postulated to cleave the N-OH bond of N-hydroxylated substrates in concert with electron transfer from NADH to cytochrome b5 reductase then to cytochrome b5, the ultimate electron donor that primes the active site for substrate reduction (PubMed:21029045, PubMed:19053771). {ECO:0000269|PubMed:19053771, ECO:0000269|PubMed:21029045, ECO:0000269|PubMed:30397129}. |
| Pathway | |
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| Tissue Specificity |
QC Data
| Note | Please contact us for QC Data |
| Product Image (Reference Only) |  |