Datasheet

Biological Description

Specificity	Anti-CYP2E1 Mouse Antibody [F19L7] detects endogenous levels of total CYP2E1 protein.
Background	Cytochrome P450 2E1 (CYP2E1), an ethanol-metabolizing enzyme, is a member of the cytochrome P450 superfamily of heme-containing monooxygenases that catalyze the oxidative metabolism of a wide range of endogenous and exogenous compounds. Structurally, CYP2E1 is an endoplasmic reticulum–anchored enzyme composed of a hydrophobic N-terminal membrane-binding domain and a conserved catalytic heme-binding domain that facilitates electron transfer from NADPH–cytochrome P450 reductase to substrates. It is constitutively expressed at high levels in the liver, but is also found in lung, kidney, brain, nasal mucosa, small intestine, and testes, with expression inducible by ethanol, nicotine, fasting, and various xenobiotics. Functionally, CYP2E1 plays a dual role: it metabolizes physiologic substrates such as fatty acids and ketone bodies, while also bioactivating a variety of drugs (e.g., acetaminophen, chlorzoxazone, halothane) and environmental toxins (e.g., benzene, nitrosamines, 1,3-butadiene) into reactive intermediates. This enzymatic activity contributes to both detoxification and carcinogenesis, as CYP2E1 generates DNA-reactive metabolites and reactive oxygen species (ROS), thereby mediating oxidative stress, lipid peroxidation, and cytotoxicity. Its inducible nature and tissue-specific expression make CYP2E1 a critical determinant of chemical toxicity, cancer risk, and inter-individual variability in drug metabolism.

Specificity

Anti-CYP2E1 Mouse Antibody [F19L7] detects endogenous levels of total CYP2E1 protein.

Background

Cytochrome P450 2E1 (CYP2E1), an ethanol-metabolizing enzyme, is a member of the cytochrome P450 superfamily of heme-containing monooxygenases that catalyze the oxidative metabolism of a wide range of endogenous and exogenous compounds. Structurally, CYP2E1 is an endoplasmic reticulum–anchored enzyme composed of a hydrophobic N-terminal membrane-binding domain and a conserved catalytic heme-binding domain that facilitates electron transfer from NADPH–cytochrome P450 reductase to substrates. It is constitutively expressed at high levels in the liver, but is also found in lung, kidney, brain, nasal mucosa, small intestine, and testes, with expression inducible by ethanol, nicotine, fasting, and various xenobiotics. Functionally, CYP2E1 plays a dual role: it metabolizes physiologic substrates such as fatty acids and ketone bodies, while also bioactivating a variety of drugs (e.g., acetaminophen, chlorzoxazone, halothane) and environmental toxins (e.g., benzene, nitrosamines, 1,3-butadiene) into reactive intermediates. This enzymatic activity contributes to both detoxification and carcinogenesis, as CYP2E1 generates DNA-reactive metabolites and reactive oxygen species (ROS), thereby mediating oxidative stress, lipid peroxidation, and cytotoxicity. Its inducible nature and tissue-specific expression make CYP2E1 a critical determinant of chemical toxicity, cancer risk, and inter-individual variability in drug metabolism.

Usage Information

Application

WB, IHC, IF, ELISA

Dilution

WB	IHC	IF
1:1000-1:6000	1:500-1:2000	1:400-1:1600

Reactivity

Mouse, Rat, Pig

Source

Mouse

MW

57 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/16368115/
https://pubmed.ncbi.nlm.nih.gov/10418964/

Anti-CYP2E1 Mouse Antibody [F19L7]

Biological Description

Usage Information

References

Application Data