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C5614

Sigma-Aldrich

Cytochrome P450 human

1A2 Isozyme Microsomes, with P450 Reductase and cytochrome b5, recombinant, expressed in baculovirus infected insect cells (BTI-TN-5B1-4)

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About This Item

Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

human

Niveau de qualité

Produit recombinant

expressed in baculovirus infected insect cells (BTI-TN-5B1-4)

Forme

solution

Poids mol.

58 kDa

Conditionnement

vial of 0.5 nmol

Numéro d'accès UniProt

Application(s)

cell analysis

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

human ... CYP1A2(1544)

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Application

Human cytochrome P450 has been used in a study to investigate non-viral environmental risk factors for nasopharyngeal carcinoma. Human cytochrome P450 has also been used in a study to investigate the dynamics and hydration of the active sites of mammalian cytochromes.

Actions biochimiques/physiologiques

Cytochrome P450 enzymes are heme containing monooxygenases which are found primarily in the mammalian liver. They catalyze the oxidative metabolism of xenobiotics. This metabolism is the initial step in the biotransformation and elimination of a wide variety of drugs and environmental pollutants from the body. This product has a molecular mass of approximately 58 kDa. Amiodarone, furafylline, and cimetidine are inhibitors, whereas tobacco, insulin, and omeprazole are inducers of the enzyme. The isozyme CYP1A2 is a major pathway for the 6-hydroxylation of melatonin in vivo. This isozyme also catalyzes the 5-hydroxylation of thiabendazole.
Cytochrome P450 is a heterogeneous family of isozymes whose primary function is to oxidize small molecules, both as a function of intermediary metabolism (e.g., fatty acids) and to detoxify exogenous compounds (drugs or toxins). Some isoforms have narrow substrate specificity, while others are promiscuous.

Autres remarques

Microsomes containing recombinant human CYP1A2, recombinant rabbit NADPH-P450 reductase, and cytochrome b5.

Forme physique

Solution in 100 mM potassium phosphate buffer, pH 7.4.

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Wei-Hua Jia et al.
Seminars in cancer biology, 22(2), 117-126 (2012-02-09)
This review aims to systematically summarize the epidemiological studies on nasopharyngeal carcinoma (NPC) conducted over the past half century, covering descriptive epidemiological studies and reports on non-viral risk factors. Multiple lines of epidemiologic evidence for established risk factors are systematically
Li Li et al.
Protein and peptide letters, 19(1), 57-61 (2011-09-17)
Human cytochrome P450(CYP 450) enzymes mediate over 60% of the phase I-dependent metabolism of clinical drugs. They are also known for the polymorphism functions that have significant impacts on the enzyme activities. In this study, a web-server called SCYPPred was
Tereza Hendrychova et al.
Current drug metabolism, 13(2), 177-189 (2012-01-03)
The flexibility, active site volume, solvation, and access path dynamics of six metabolically active mammalian cytochromes P450 (human 2A6, 2C9, 2D6, 2E1, 3A4 and rabbit 2B4) are extensively studied using molecular dynamics (MD) simulations. On average, the enzymes' overall structures
Moritz Walter et al.
Toxicology in vitro : an international journal published in association with BIBRA, 59, 215-220 (2019-04-21)
Next to its well-studied toxicity, carbon monoxide (CO) is recognized as a signalling molecule in various cellular processes. Thus, CO-releasing molecules (CORMs) are of considerable interest for basic research and drug development. Aim of the present study was to investigate
Xiangrong Zhang et al.
PloS one, 9(4), e94962-e94962 (2014-04-17)
The present study characterized in vitro metabolites of 20(R)-25-methoxyl-dammarane-3β, 12β, 20-triol (20(R)-25-OCH3-PPD) in mouse, rat, dog, monkey and human liver microsomes. 20(R)-25-OCH3-PPD was incubated with liver microsomes in the presence of NADPH. The reaction mixtures and the metabolites were identified

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