E9788
Cytochrome P450 1A2 human
recombinant, expressed in Saccharomyces cerevisiae
Sinónimos:
Cytochrome P450 Microsome Preparation human, Cerosomes
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About This Item
Productos recomendados
biological source
human
Quality Level
recombinant
expressed in Saccharomyces cerevisiae
form
liquid
specific activity
≥0.5 units/pmol enzyme
secondary activity
≥100 units/mg protein (Reductase activity)
concentration
≥1 pmol/μL (P450)
≥10 mg/mL protein
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... CYP1A2(1544)
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General description
Microsome contents of CYP1A2 human and yeast CYP-reductase expressed in Saccharomyces cerevisiae.
Unit Definition
P450 Activity: One unit will oxidize 1 picomole of ethoxyresorufin per minute at pH 7.4 at 28 °C.
Reductase Activity: One unit will reduce 1 nanomole of cytochrome C per minute in the presence of NADPH at pH 7.4 at 28 °C.
Reductase Activity: One unit will reduce 1 nanomole of cytochrome C per minute in the presence of NADPH at pH 7.4 at 28 °C.
Physical form
50 mM Tris (pH 7.4), 1 mM EDTA, 20% glycerol
Other Notes
For more more information visit our drug metabolism resources for Cytochrome P450 microsome preparations.
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Micromachines, 9(12) (2018-12-14)
This work describes the interfacing of electrowetting-on-dielectric based digital microfluidic (DMF) sample preparation devices with ambient mass spectrometry (MS) via desorption atmospheric pressure photoionization (DAPPI). The DMF droplet manipulation technique was adopted to facilitate drug distribution and metabolism assays in
Drug metabolism and pharmacokinetics, 30(3), 247-252 (2015-05-30)
Genetic variations in cytochrome P450 1A2 (CYP1A2) are associated with interindividual variability in the metabolism and efficacy of many medications. Twenty CYP1A2 variants harboring amino acid substitutions were analyzed for functional changes in enzymatic activity. Recombinant CYP1A2 variant proteins were
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