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Mouse Anti-CYP2C9 Recombinant Antibody (CBLC-LY-020) (V2LY-0125-LY955)


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Published Data
V2LY-0125-LY955-1
Mouse Anti-CYP2C9 Recombinant Antibody (CBLC-LY-020) (V2LY-0125-LY955) in IHC
IHC of the zone 3-specific CYPs CYP1A2 and CYP3A4. Sections were counterstained with an antibody against human CYP2C, which does not show strong zone specificity. Nuclei were also counterstained with DAPI in merged images. Images of sections transplanted with hCLiPs derived from lot FCL are shown as representative data. ...View More
Katsuda, T., Matsuzaki, J., Yamaguchi, T., Yamada, Y., Prieto-Vila, M., Hosaka, K., ... & Ochiya, T. (2019). Generation of human hepatic progenitor cells with regenerative and metabolic capacities from primary hepatocytes. Elife, 8, e47313. Distributed under Open Access license CC BY 4.0, without modification.

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
CBLC-LY-020
Antibody Isotype
IgG1, κ
Application
WB, IP, IF, ELISA, IHC-P

Basic Information

Immunogen
CYP2C6 purified from rat liver.
Host Species
Mouse
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1, κ
Clonality
Monoclonal Antibody
Application Notes
ApplicationNote
WB1:100-1:1,000
IP1-2 μg per 100-500 μg of total protein (1 mL of cell lysate)
IF(ICC)1:50-1:500
ELISA1:100-1:1,000
IHC-P1:50-1:500

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
Gelatin & PBS
Preservative
Sodium Azide
Concentration
0.2 mg/mL
Purity
>95% as determined by analysis by SDS-PAGE
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Cytochrome P450 Family 2 Subfamily C Member 9
Entrez Gene ID
1559
UniProt ID
P11712
Function
A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids and steroids (PubMed:7574697, PubMed:9866708, PubMed:9435160, PubMed:12865317, PubMed:15766564, PubMed:19965576, PubMed:21576599).

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) (PubMed:7574697, PubMed:9866708, PubMed:9435160, PubMed:12865317, PubMed:15766564, PubMed:19965576, PubMed:21576599).

Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA) (PubMed:7574697, PubMed:15766564, PubMed:19965576, PubMed:9866708).

Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis (PubMed:21576599).

Exhibits low catalytic activity for the formation of catechol estrogens from 17beta-estradiol (E2) and estrone (E1), namely 2-hydroxy E1 and E2 (PubMed:12865317).

Catalyzes bisallylic hydroxylation and hydroxylation with double-bond migration of polyunsaturated fatty acids (PUFA) (PubMed:9866708, PubMed:9435160).

Also metabolizes plant monoterpenes such as limonene. Oxygenates (R)- and (S)-limonene to produce carveol and perillyl alcohol (PubMed:11950794).

Contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S-warfarin, diclofenac, phenytoin, tolbutamide and losartan (PubMed:25994031).
Biological Process
Cellular amide metabolic process Source: BHF-UCL
Cholesterol metabolic process Source: UniProtKB-UniPathway
Drug catabolic process Source: BHF-UCL
Drug metabolic process Source: BHF-UCL
Epoxygenase P450 pathway Source: UniProtKB
Estrogen metabolic process Source: UniProtKB
Exogenous drug catabolic process Source: BHF-UCL
Icosanoid biosynthetic process Source: UniProtKB
Long-chain fatty acid biosynthetic process Source: Reactome
Monocarboxylic acid metabolic process Source: BHF-UCL
Monoterpenoid metabolic process Source: BHF-UCL
Omega-hydroxylase P450 pathway Source: Reactome
Organic acid metabolic process Source: GO_Central
Oxidative demethylation Source: BHF-UCL
Steroid metabolic process Source: BHF-UCL
Urea metabolic process Source: BHF-UCL
Xenobiotic metabolic process Source: GO_Central
Cellular Location
Endoplasmic reticulum membrane; Microsome membrane
More Infomation

Sangkuhl, K., Claudio‐Campos, K., Cavallari, L. H., Agundez, J. A., Whirl‐Carrillo, M., Duconge, J., ... & Gaedigk, A. (2021). PharmVar GeneFocus: CYP2C9. Clinical Pharmacology & Therapeutics, 110(3), 662-676.

Amorosi, C. J., Chiasson, M. A., McDonald, M. G., Wong, L. H., Sitko, K. A., Boyle, G., ... & Dunham, M. J. (2021). Massively parallel characterization of CYP2C9 variant enzyme activity and abundance. The American Journal of Human Genetics, 108(9), 1735-1751.

Chen, H., Dai, D. P., Zhou, S., Liu, J., Wang, S. H., Wu, H. L., ... & Yang, J. F. (2020). An identification and functional evaluation of a novel CYP2C9 variant CYP2C9* 62. Chemico-Biological Interactions, 327, 109168.

Theken, K. N., Lee, C. R., Gong, L., Caudle, K. E., Formea, C. M., Gaedigk, A., ... & Grosser, T. (2020). Clinical Pharmacogenetics Implementation Consortium Guideline (CPIC) for CYP2C9 and nonsteroidal anti‐inflammatory drugs. Clinical Pharmacology & Therapeutics, 108(2), 191-200.

Monostory, K., Nagy, A., Tóth, K., Bűdi, T., Kiss, Á., Déri, M., & Csukly, G. (2019). Relevance of CYP2C9 function in valproate therapy. Current neuropharmacology, 17(1), 99-106.

Louet, M., Labbé, C. M., Fagnen, C., Aono, C. M., Homem-de-Mello, P., Villoutreix, B. O., & Miteva, M. A. (2018). Insights into molecular mechanisms of drug metabolism dysfunction of human CYP2C9* 30. PloS one, 13(5), e0197249.

Silvado, C. E., Terra, V. C., & Twardowschy, C. A. (2018). CYP2C9 polymorphisms in epilepsy: influence on phenytoin treatment. Pharmacogenomics and Personalized Medicine, 11, 51.

Flora, D. R., Rettie, A. E., Brundage, R. C., & Tracy, T. S. (2017). CYP2C9 genotype‐dependent warfarin pharmacokinetics: impact of CYP2C9 genotype on R‐and S‐warfarin and their oxidative metabolites. The Journal of Clinical Pharmacology, 57(3), 382-393.

Daly, A. K., Rettie, A. E., Fowler, D. M., & Miners, J. O. (2017). Pharmacogenomics of CYP2C9: functional and clinical considerations. Journal of personalized medicine, 8(1), 1.

Liu, R., Lyu, X., Batt, S. M., Hsu, M. H., Harbut, M. B., Vilchèze, C., ... & Wang, F. (2017). Determinants of the Inhibition of DprE1 and CYP2C9 by Antitubercular Thiophenes. Angewandte Chemie International Edition, 56(42), 13011-13015.

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For research use only. Not intended for any clinical use.

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