C3735
Cytochrome P450 human
1A1 Isozyme Microsomes, with P450 Reductase, recombinant, expressed in baculovirus infected insect cells (BTI-TN-5B1-4)
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About This Item
Numéro MDL:
Code UNSPSC :
12161501
Nomenclature NACRES :
NA.47
Produits recommandés
Source biologique
human
Niveau de qualité
Produit recombinant
expressed in baculovirus infected insect cells (BTI-TN-5B1-4)
Forme
solution
Activité spécifique
≥4 units/pmol enzyme
Poids mol.
45-60 kDa
Conditionnement
vial of 0.5 nmol
Technique(s)
activity assay: suitable
Solubilité
water: soluble
Adéquation
suitable for molecular biology
Numéro d'accès UniProt
Application(s)
cell analysis
Conditions d'expédition
dry ice
Température de stockage
−70°C
Informations sur le gène
human ... CYP1A1(1543)
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Description générale
Research area: Immuno and CKS
Cytochrome P450 (CYP) enzymes are a family of enzymes that are encoded by the P450 genes. These enzymes are membrane bound hemoproteins. that are mainly found in the liver’s endoplasmic reticulum.
Cytochrome P450 (CYP) enzymes are a family of enzymes that are encoded by the P450 genes. These enzymes are membrane bound hemoproteins. that are mainly found in the liver’s endoplasmic reticulum.
Actions biochimiques/physiologiques
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. The CYP1A1 isoform catalyzes 7-deethylation of ethoxyresorufin. Cytochrome P450 (CYP) plays an important role in detoxifying xenobiotics, cellular metabolism and homeostasis. One of the main mechanisms of drug-drug interactions is the induction or inhibition of these enzymes. CYP enzymes are transcriptionally activated by a variety of xenobiotics and by endogenous substrates via receptor-dependent pathways. Inhibition of these enzymes is a major factor in metabolism-based drug-drug interactions, and many chemotherapeutic medications can cause drug interactions by either inhibiting or inducing the cytochrome p450 enzyme system.
Forme physique
Solution in 100 mM potassium phosphate buffer, pH 7.4.
Notes préparatoires
Microsomes containing human CYP1A1 and recombinant human NADPH-P450 reductase.
Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 2
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Les clients ont également consulté
Tomas Erban et al.
Biomedical chromatography : BMC, 26(9), 1062-1065 (2011-11-29)
A 96-well microplate-based HPLC endpoint assay is described for the determination of NADPH-cytochrome P450 reductase (CPR) activity. Novel sampling of NADPH into microplates was optimized. Separation was performed on a Zorbax Eclipse XDB-C₁₈ analytical 4.6 × 150 mm, 5 µm column. To validate the
Palrasu Manikandan et al.
Current drug targets, 19(1), 38-54 (2017-01-27)
The cytochrome P450 (CYP) enzymes are membrane-bound hemoproteins that play a pivotal role in the detoxification of xenobiotics, cellular metabolism and homeostasis. Induction or inhibition of CYP enzymes is a major mechanism that underlies drug-drug interactions. CYP enzymes can be
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
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Archives of biochemistry and biophysics, 687, 108383-108383 (2020-04-27)
Intracellular carbon monoxide (CO) is a gaseous signaling molecule and is generated enzymatically by heme oxygenases upon degradation of heme to billiverdin. Target structures for intracellular produced CO are heme proteins including cytochrome c oxidase of the respiratory chain, cytochrome
D P Bofinger et al.
Toxicological sciences : an official journal of the Society of Toxicology, 62(2), 299-314 (2001-07-14)
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