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Merck

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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A propos de cet article

UNSPSC Code:
12161501
NACRES:
NA.47
Numéro CE :
MDL number:
Specific activity:
≥4 units/pmol enzyme
Biological source:
human
Recombinant:
expressed in baculovirus infected insect cells (BTI-TN-5B1-4)
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biological source

human

recombinant

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

form

solution

specific activity

≥4 units/pmol enzyme

mol wt

45-60 kDa

packaging

vial of 0.5 nmol

technique(s)

activity assay: suitable

solubility

water: soluble

suitability

suitable for molecular biology

UniProt accession no.

application(s)

cell analysis

shipped in

dry ice

storage temp.

−70°C

Quality Level

Gene Information

human ... CYP1A1(1543)

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General description

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.

Biochem/physiol Actions

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.

Physical form

Solution in 100 mM potassium phosphate buffer, pH 7.4.

Preparation Note

Microsomes containing human CYP1A1 and recombinant human NADPH-P450 reductase.

Classe de stockage

12 - Non Combustible Liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
D P Bofinger et al.
Toxicological sciences : an official journal of the Society of Toxicology, 62(2), 299-314 (2001-07-14)
Endometriosis is a debilitating disease estimated to affect 10% of reproductive-age women and characterized by the growth of endometrial tissue outside of the uterus. The present study characterizes a human endometrial explant culture model for studying the direct effects of
David Stucki et al.
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

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