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Mouse Anti-CYP3A4 Recombinant Antibody (3H8) (CBMAB-C6358-LY)

This product is antibody recognizes CYP3A4. The antibody 3H8 immunoassay techniques such as: FC, ELISA, ICC/IF, IHC-P, WB.
See all CYP3A4 antibodies
Published Data

Summary

Host Animal
Mouse
Specificity
Human
Clone
3H8
Antibody Isotype
IgG1
Application
FC, ELISA, ICC/IF, IHC-P, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
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 3 Subfamily A Member 4
Introduction
CYP3A4 (Cytochrome P450 Family 3 Subfamily A Member 4) is a Protein Coding gene. Diseases associated with CYP3A4 include Acetaminophen Metabolism and Tacrolimus Dose Selection. Among its related pathways are Gefitinib Pathway, Pharmacokinetics and Metformin Pathway, Pharmacodynamics. Gene Ontology (GO) annotations related to this gene include enzyme binding and iron ion binding.
An important paralog of this gene is CYP3A7.
Entrez Gene ID
UniProt ID
Alternative Names
Cytochrome P450 Family 3 Subfamily A Member 4; Cytochrome P450, Subfamily IIIA (Niphedipine Oxidase), Polypeptide 4; Cytochrome P450, Family 3, Subfamily A, Polypeptide 4; Taurochenodeoxycholate 6-Alpha-Hydroxylase; 1,8-Cineole 2-Exo-Monooxygenase; Cholesterol 25-Hydroxylase; Albendazole Monooxygenase; Albendazole Sulfoxidase; Quinine 3-Monooxygenase; Cytochrome P450 NF-25; Cytochrome P450-PCN1; Cytochrome P450 3A3; Cytochrome P450 HLp; Nifedipine Oxidase; EC 1.14.14.1; CYPIIIA3; CYPIIIA4; CYP3A3;
Function
A cytochrome P450 monooxygenase involved in the metabolism of sterols, steroid hormones, retinoids and fatty acids (PubMed:10681376, PubMed:11093772, PubMed:11555828, PubMed:14559847, PubMed:12865317, PubMed:15373842, PubMed:15764715, PubMed:20702771, PubMed:19965576, PubMed:21490593, 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). Catalyzes the hydroxylation of carbon-hydrogen bonds (PubMed:2732228, PubMed:14559847, PubMed:12865317, PubMed:15373842, PubMed:15764715, PubMed:21576599, PubMed:21490593).

Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C-16 position (PubMed:11555828, PubMed:14559847, PubMed:12865317).

Plays a role in the metabolism of androgens, particularly in oxidative deactivation of testosterone (PubMed:2732228, PubMed:15373842, PubMed:15764715, PubMed:22773874).

Metabolizes testosterone to less biologically active 2beta- and 6beta-hydroxytestosterones (PubMed:2732228, PubMed:15373842, PubMed:15764715).

Contributes to the formation of hydroxycholesterols (oxysterols), particularly A-ring hydroxylated cholesterol at the C-4beta position, and side chain hydroxylated cholesterol at the C-25 position, likely contributing to cholesterol degradation and bile acid biosynthesis (PubMed:21576599).

Catalyzes bisallylic hydroxylation of polyunsaturated fatty acids (PUFA) (PubMed:9435160).

Catalyzes the epoxidation of double bonds of PUFA with a preference for the last double bond (PubMed:19965576).

Metabolizes endocannabinoid arachidonoylethanolamide (anandamide) to 8,9-, 11,12-, and 14,15-epoxyeicosatrienoic acid ethanolamides (EpETrE-EAs), potentially modulating endocannabinoid system signaling (PubMed:20702771).

Plays a role in the metabolism of retinoids. Displays high catalytic activity for oxidation of all-trans-retinol to all-trans-retinal, a rate-limiting step for the biosynthesis of all-trans-retinoic acid (atRA) (PubMed:10681376).

Further metabolizes atRA toward 4-hydroxyretinoate and may play a role in hepatic atRA clearance (PubMed:11093772).

Responsible for oxidative metabolism of xenobiotics. Acts as a 2-exo-monooxygenase for plant lipid 1,8-cineole (eucalyptol) (PubMed:11159812).

Metabolizes the majority of the administered drugs. Catalyzes sulfoxidation of the anthelmintics albendazole and fenbendazole (PubMed:10759686).

Hydroxylates antimalarial drug quinine (PubMed:8968357).

Acts as a 1,4-cineole 2-exo-monooxygenase (PubMed:11695850).

Also involved in vitamin D catabolism and calcium homeostasis. Catalyzes the inactivation of the active hormone calcitriol (1-alpha,25-dihydroxyvitamin D3) (PubMed:29461981).
Biological Process
Aflatoxin metabolic process Source: Reactome
Alkaloid catabolic process Source: BHF-UCL
Androgen metabolic process Source: BHF-UCL
Cholesterol metabolic process Source: UniProtKB-UniPathway
Drug catabolic process Source: BHF-UCL
Drug metabolic process Source: BHF-UCL
Estrogen metabolic process Source: UniProtKB
Exogenous drug catabolic process Source: BHF-UCL
Heterocycle metabolic process Source: BHF-UCL
Lipid hydroxylation Source: BHF-UCL
Lipid metabolic process Source: ProtInc
Long-chain fatty acid biosynthetic process Source: Reactome
Monoterpenoid metabolic process Source: BHF-UCL
Oxidative demethylation Source: BHF-UCL
Retinoic acid metabolic process Source: UniProtKB
Retinol metabolic process Source: UniProtKB
Steroid catabolic process Source: BHF-UCL
Steroid metabolic process Source: BHF-UCL
Vitamin D catabolic process Source: UniProtKB
Vitamin D metabolic process Source: BHF-UCL
Xenobiotic metabolic process Source: Reactome
Cellular Location
Endoplasmic reticulum membrane; Microsome membrane
Involvement in disease
Vitamin D-dependent rickets 3 (VDDR3):
An autosomal dominant disorder of vitamin D metabolism resulting in early-onset rickets, reduced serum levels of the vitamin D metabolites 25-hydroxyvitamin D and 1,25-dihydroxyvitamin D, and deficient responsiveness to parent and activated forms of vitamin D.
Topology
Helical: 2-22
PTM
Polyubiquitinated in the presence of AMFR and UBE2G1 and also STUB1/CHIP and UBE2D1 (in vitro).

Liu, X. Y., Guo, Z. T., Chen, Z. D., Zhang, Y. F., Zhou, J. L., Jiang, Y., ... & Zhong, D. F. (2020). Alflutinib (AST2818), primarily metabolized by CYP3A4, is a potent CYP3A4 inducer. Acta Pharmacologica Sinica, 41(10), 1366-1376.

Bulutoglu, B., Rey-Bedón, C., Mert, S., Tian, L., Jang, Y. Y., Yarmush, M. L., & Usta, O. B. (2020). A comparison of hepato-cellular in vitro platforms to study CYP3A4 induction. PloS one, 15(2), e0229106.

Harskamp, R. E., Teichert, M., Lucassen, W. A., van Weert, H. C., & Lopes, R. D. (2019). Impact of polypharmacy and P-glycoprotein-and CYP3A4-modulating drugs on safety and efficacy of oral anticoagulation therapy in patients with atrial fibrillation. Cardiovascular drugs and therapy, 33(5), 615-623.

Ebmeyer, J., Braeuning, A., Glatt, H., These, A., Hessel-Pras, S., & Lampen, A. (2019). Human CYP3A4-mediated toxification of the pyrrolizidine alkaloid lasiocarpine. Food and Chemical Toxicology, 130, 79-88.

Ning, J., Wang, W., Ge, G., Chu, P., Long, F., Yang, Y., ... & James, T. D. (2019). Target Enzyme‐Activated Two‐Photon Fluorescent Probes: A Case Study of CYP3A4 Using a Two‐Dimensional Design Strategy. Angewandte Chemie, 131(29), 10064-10068.

Jamwal, R., de la Monte, S. M., Ogasawara, K., Adusumalli, S., Barlock, B. B., & Akhlaghi, F. (2018). Nonalcoholic fatty liver disease and diabetes are associated with decreased CYP3A4 protein expression and activity in human liver. Molecular pharmaceutics, 15(7), 2621-2632.

Lolodi, O., Wang, Y. M., Wright, W. C., & Chen, T. (2017). Differential regulation of CYP3A4 and CYP3A5 and its implication in drug discovery. Current drug metabolism, 18(12), 1095-1105.

Ashida, R., Okamura, Y., Ohshima, K., Kakuda, Y., Uesaka, K., Sugiura, T., ... & Yamaguchi, K. (2017). CYP3A4 gene is a novel biomarker for predicting a poor prognosis in hepatocellular carcinoma. Cancer genomics & proteomics, 14(6), 445-453.

Ouatas, T., Duval, V., Sinclair, K., & Berkowitz, N. (2017). Concomitant use of midostaurin with strong CYP3A4 inhibitors: an analysis from the ratify trial. Blood, 130, 3814.

Lv, X., Pan, L., Wang, J., Lu, L., Yan, W., Zhu, Y., ... & Zhuang, S. (2017). Effects of triazole fungicides on androgenic disruption and CYP3A4 enzyme activity. Environmental pollution, 222, 504-512.

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

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