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CYP2C9 Protein, Human, Recombinant (His & Myc)

Catalog No. TMPH-01186

CYP2C9 Protein, Human, Recombinant (His & Myc) is expressed in E. coli.

CYP2C9 Protein, Human, Recombinant (His & Myc)

CYP2C9 Protein, Human, Recombinant (His & Myc)

Catalog No. TMPH-01186
CYP2C9 Protein, Human, Recombinant (His & Myc) is expressed in E. coli.
Pack SizePriceAvailabilityQuantity
20 μg$28420 days
100 μg$53720 days
1 mg$2,30020 days
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Product Information

Biological Activity
Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description
CYP2C9 Protein, Human, Recombinant (His & Myc) is expressed in E. coli.
Species
Human
Expression System
E. coli
TagN-10xHis, C-Myc
Accession NumberP11712
Synonyms
S-mephenytoin 4-hydroxylase,Cytochrome P-450MP,Cytochrome P450 PB-1,Cytochrome P450 MP-8,Cytochrome P450 MP-4,Cytochrome P450 2C9,CYPIIC9,CYP2C9,CYP2C10,Cholesterol 25-hydroxylase,(S)-limonene 7-monooxygenase,(S)-limonene 6-monooxygenase,(R)-limonene 6-monooxygenase
Amino Acid
MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKVYGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKWKEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKGG
Construction
1-162 aa
Protein Purity
> 85% as determined by SDS-PAGE.
Molecular Weight25.4 kDa (predicted)
FormulationTris-based buffer, 50% glycerol
Reconstitution
A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
Stability & Storage
Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
ShippingIn general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.
Research Background
A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids and steroids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA). Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. Exhibits low catalytic activity for the formation of catechol estrogens from 17beta-estradiol (E2) and estrone (E1), namely 2-hydroxy E1 and E2. Catalyzes bisallylic hydroxylation and hydroxylation with double-bond migration of polyunsaturated fatty acids (PUFA). Also metabolizes plant monoterpenes such as limonene. Oxygenates (R)- and (S)-limonene to produce carveol and perillyl alcohol. Contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S-warfarin, diclofenac, phenytoin, tolbutamide and losartan.

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Please read the User Guide of Recombinant Proteins for more specific information.