NAD(P)H-flavin reductase Protein, E.coli (His)
Based on 1 publication(s) in Google Scholar
The NAD(P)H-flavin reductase protein plays a key role in cellular redox processes by catalyzing the reduction of soluble flavins using reduced pyridine nucleotides. This enzyme activity reflects its ability to transfer electrons from NAD(P)H to flavin, participating in important intracellular redox reactions. NAD (P) H-flavin reductase Protein, E.coli (His) is the recombinant E. coli-derived NAD(P)H-flavin reductase protein, expressed by E. coli , with N-His labeled tag.
- Species: E.coli
- Source: E. coli
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Storage:Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Biological Activity
Description
The NAD(P)H-flavin reductase protein plays a key role in cellular redox processes by catalyzing the reduction of soluble flavins using reduced pyridine nucleotides. This enzyme activity reflects its ability to transfer electrons from NAD(P)H to flavin, participating in important intracellular redox reactions. NAD (P) H-flavin reductase Protein, E.coli (His) is the recombinant E. coli-derived NAD(P)H-flavin reductase protein, expressed by E. coli , with N-His labeled tag.
Background
The NAD(P)H-flavin reductase protein is an enzyme that catalyzes the reduction of soluble flavins using reduced pyridine nucleotides, such as NADH or NADPH. This enzymatic activity is crucial for maintaining cellular redox balance and is involved in various metabolic processes where flavin coenzymes serve as electron carriers. By utilizing reduced pyridine nucleotides, NAD(P)H-flavin reductase plays a key role in transferring electrons to flavins, thereby contributing to the regulation of cellular oxidative stress and the redox state. This enzyme's involvement in flavin reduction underscores its significance in diverse biological pathways and highlights its role in modulating cellular responses to oxidative conditions.
Publications (1)
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Journal Impact Factor
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Most Recent
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Microb Biotechnol
Novel Anthraquinone Chlorination Contributes to Pigmentation and ATP Formation in Thermomyces dupontii. [Abstract]2025 Oct;18(10):e70254. PMID: 41123250
Technical Parameters
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Species E.coli
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Source E. coli
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Tag N-His
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Accession
P0AEN1 (T2-I233)
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Gene ID948325 [NCBI]
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Molecular Construction
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N-term
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His
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FRE_ECOLI (T2-I233)
Accession # P0AEN1 -
C-term
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Protein Length
Full Length
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Synonyms
FRZB; FZRB; Frizzled Related Protein; HFIZ; Secreted Frizzled-Related Protein 3; Frezzled; FRZB1; SFRP-3; SFRP3; FrzB-1; FRE; Uncharacterized Protein FRZB; Frizzled-Related Protein 1; Frizzled Homolog-Related; FRZB-PEN; Frizzled-Related Protein; FRZB-1; F
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AA Sequence
TTLSCKVTSVEAITDTVYRVRIVPDAAFSFRAGQYLMVVMDERDKRPFSMASTPDEKGFIELHIGASEINLYAKAVMDRILKDHQIVVDIPHGEAWLRDDEERPMILIAGGTGFSYARSILLTALARNPNRDITIYWGGREEQHLYDLCELEALSLKHPGLQVVPVVEQPEAGWRGRTGTVLTAVLQDHGTLAEHDIYIAGRFEMAKIARDLFCSERNAREDRLFGDAFAFI
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Predicted Molecular Mass
30.1 kDa
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Molecular Weight
Approximately 30 kDa, based on SDS-PAGE under reducing conditions.
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Purity
≥ 90%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder
Lyophilized from a 0.22 μm filtered solution of PBS, 6% Trehalose, pH 7.4.
<1 EU/μg, determined by LAL method.
It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O.
Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Room temperature in continental US; may vary elsewhere.
Documentation
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Data Sheet (236 KB)
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SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
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Handling Instructions (2659 KB)
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)