C8113
Cytochrome P450 Reductase human
recombinant, expressed in baculovirus infected insect cells
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Synonym(s):
NADPH: Ferrihemoprotein oxidoreductase
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
recombinant
expressed in baculovirus infected insect cells
Quality Level
form
solution
specific activity
≥30 U/mg
mol wt
calculated mol wt 76.5 kDa
concentration
≥0.5 mg/mL
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... POR(5447)
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General description
This human, recombinant protein is isolated from insect cells infected with a baculovirus containing the cDNA for human cytochrome P450 reductase. It is purified by affinity chromatography.
Application
Human cytochrome P450 reductase has been used in a study to assess the biocatalytic synthesis and structure elucidation of cyclized metabolites of the deacetylase inhibitor panobinostat (LBH589). Human cytochrome P450 reductase has also been used in a study to investigate the effects of coupled motions on electrons along the human microsomal P450 chains.
The enzyme from sigma has been used in the hypoxic and oxic reductions of the anticancer prodrug, 1,2-bis(methylsulfonyl)-1-(2-chloroethyl)-2-[[1-(4-nitrophenyl)ethoxy]carbonyl]hydrazine (KS119).
NADPH-P450 reductase is a membrane-bound flavoprotein that transfers electrons from NADPH to the various isoforms of cytochrome P450. The ratio of reductase:P450 that is typically used ranges from 0.5-5:1. The enzyme contains one mole each of FAD and FMN per mole of protein.
Biochem/physiol Actions
Cytochrome P450 reductase is a membrane bound enzyme required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. The cytochrome P450 enzyme system is mainly involved in the detoxification of xenobiotics in the liver. It also participates in the activation of procarcinogens and the metabolism of endogeneous substrates such as steroids.
Unit Definition
One unit will cause the reduction of 1.0 μmole of cytochrome c by NADPH per minute at pH 7.4 at 37 °C.
Physical form
Supplied in a solution containing 10 mM potassium phosphate, pH 7.4, 0.1 mM EDTA, 0.5 mM DTT, 20% (v/v) glycerol
WGK
WGK 2
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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Y Yasukochi et al.
The Journal of biological chemistry, 251(17), 5337-5344 (1976-09-10)
NADPH-cytochrome c (cytochrome P-450) reductase (EC 1.6.2.4) has been purified to homogeneity, as judged by sodium dodecyl sulfate disc gel electrophoresis, from detergent-solubilized rat and pig liver microsomes using an affinity chromatography procedure. Treatment of microsomes with a polyethoxynonylphenyl ether
Bas van de Waterbeemd et al.
PloS one, 8(5), e65157-e65157 (2013-06-07)
An improved detergent-free process has been developed to produce vaccine based on native outer membrane vesicles (NOMV) against Neisseria meningitidis serogroup B. Performance was evaluated with the NonaMen vaccine concept, which provides broad coverage based on nine distinct PorA antigens.
Shusuke Nambu et al.
The Journal of biological chemistry, 288(14), 10101-10109 (2013-02-20)
MhuD is an oxygen-dependent heme-degrading enzyme from Mycobacterium tuberculosis with high sequence similarity (∼45%) to Staphylococcus aureus IsdG and IsdI. Spectroscopic and mutagenesis studies indicate that the catalytically active 1:1 heme-MhuD complex has an active site structure similar to those
Masakazu Sugishima et al.
Proceedings of the National Academy of Sciences of the United States of America, 111(7), 2524-2529 (2014-02-20)
NADPH-cytochrome P450 oxidoreductase (CPR) supplies electrons to various heme proteins including heme oxygenase (HO), which is a key enzyme for heme degradation. Electrons from NADPH flow first to flavin adenine dinucleotide, then to flavin mononucleotide (FMN), and finally to heme
Christopher R Pudney et al.
PLoS biology, 9(12), e1001222-e1001222 (2011-12-30)
Protein domain motion is often implicated in biological electron transfer, but the general significance of motion is not clear. Motion has been implicated in the transfer of electrons from human cytochrome P450 reductase (CPR) to all microsomal cytochrome P450s (CYPs).
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