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Agrisera
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Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
For reconstitution add 50 µL of sterile water.
Specific Species Reactivity: Arabidopsis thaliana, Chlamydomonas reinardtii, red alga Gracilaria gracilis, Hordeum vulgare, Leptodictyum riparium (Hedw.) Warnst (moss), Medicago sativa, Phaeodactylum tricornutum Bohlin accession Pt1 8.6, Panax notoginseng, Populus yunanensis Dode, Solanum lycopersicum, Solanum tuberosum, Thalassiosira sp. (diatom), Trebouxia sp., Vigna radiata, Vitis vinigera
Nitrate reductase is a molybdenum cofactor-dependent oxidoreductase that reduces nitrate to nitrite and occurs in distinct cellular locations depending on the biological context: in many bacteria, the major respiratory nitrate reductase is a cytoplasmic membrane-anchored complex with nitrate reduced at a cytoplasmically oriented catalytic site while electrons are supplied from the membrane quinol pool, whereas in plants the assimilatory NAD(P)H-dependent nitrate reductase is a soluble cytosolic enzyme that channels electrons from NAD(P)H to nitrate. Structurally, the bacterial respiratory enzyme is typically organized as a multisubunit NarGHI complex in which the extrinsic catalytic subunits (NarG and NarH) are attached to an integral membrane anchor (NarI); NarG houses the nitrate-reducing active site containing a Mo-bis(molybdopterin guanine dinucleotide) cofactor, NarH contains multiple iron-sulfur clusters that relay electrons, and NarI is a diheme b cytochrome that provides the quinol oxidation site and a conduit for electron transfer across the membrane. In contrast, eukaryotic assimilatory nitrate reductase is generally a homodimeric ~100 kDa-per-subunit enzyme composed of discrete redox domains binding FAD, a b-type heme, and a molybdenum-molybdopterin center, enabling intramolecular electron transfer from NAD(P)H via FAD and heme to the Mo active site. Functionally, these enzymes connect nitrate availability to cellular metabolism: bacterial membrane-bound nitrate reductase supports anaerobic respiration and can contribute to proton motive force generation via spatial separation of quinol oxidation and nitrate reduction, while cytosolic plant nitrate reductase catalyzes the first committed step of nitrate assimilation, governing flux into reduced nitrogen metabolism.
仅用于科研。不用于诊断过程。未经明确授权不得转售。
蛋白别名: GNR1; NIA1; NIA2; NITRATE REDUCTASE; nitrate reductase 1; NR; NR1; T32E8.9; T32E8_9