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Merck
CN

C8113

Sigma-Aldrich

Cytochrome P450 Reductase human

recombinant, expressed in baculovirus infected insect cells

Synonym(s):

NADPH: Ferrihemoprotein oxidoreductase

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About This Item

EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
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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.
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.
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).

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.

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

Other Notes

One unit will cause the reduction of 1.0 μmole of cytochrome c by NADPH per minute at pH 7.4 at 37 °C.

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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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
Chunja Lee et al.
Canadian journal of physiology and pharmacology, 90(10), 1354-1363 (2012-09-18)
The aryl hydrocarbon receptor (AHR) has physiological roles in the absence of exposure to exogenous ligands, and mediates adaptive and toxic responses to the environmental pollutant 2,3,7,8-tetracholorodibenzo-p-dioxin (TCDD). A readily metabolized AHR agonist, 3-methylcholanthrene, disrupts the expression of mouse hepatic

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