Specification
Description | Recombinant protein from the full-length sequence of Homo sapiens mitochondrial amidoxime reducing component 2 (MTARC2), transcript variant 2 (NM_017898). |
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 | Q969Z3 |
Entry Name | MARC2_HUMAN |
Gene Names | MTARC2 MARC2 MOSC2 |
Alternative Gene Names | MARC2 MOSC2 |
Alternative Protein Names | Mitochondrial amidoxime reducing component 2 (mARC2) (EC 1.7.-.-) (Molybdenum cofactor sulfurase C-terminal domain-containing protein 2) (MOSC domain-containing protein 2) (Moco sulfurase C-terminal domain-containing protein 2) |
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 | 335 |
Molecular Weight(Da) | 38023 |
Protein Sequence | (The sequence of expressed protein may have some variation from the sequence shown below. Please contact us for the exact sequence.) MGASSSSALARLGLPARPWPRWLGVAALGLAAVALGTVAWRRAWPRRRRRLQQVGTVAKLWIYPVKSCKGVPVSEAECTAMGLRSGNLRDRFWLVIKEDGHMVTARQEPRLVLISIIYENNCLIFRAPDMDQLVLPSKQPSSNKLHNCRIFGLDIKGRDCGNEAAKWFTNFLKTEAYRLVQFETNMKGRTSRKLLPTLDQNFQVAYPDYCPLLIMTDASLVDLNTRMEKKMKMENFRPNIVVTGCDAFEEDTWDELLIGSVEVKKVMACPRCILTTVDPDTGVIDRKQPLDTLKSYRLCDPSERELYKLSPLFGIYYSVEKIGSLRVGDPVYRMV |
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:21029045, PubMed:24423752). As a component of prodrug-converting system, reduces a multitude of N-hydroxylated prodrugs particularly amidoximes, leading to increased drug bioavailability (PubMed:21029045, PubMed:24423752). 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). {ECO:0000269|PubMed:21029045, ECO:0000269|PubMed:24423752}. |
Pathway | |
Protein Families | |
Tissue Specificity |
QC Data
Note | Please contact us for QC Data |
Product Image (Reference Only) | ![]() |