Rabbit Polyclonal Cytochrome P450 1A2 antibody. Suitable for IHC-P and reacts with Rat samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human CYP1A2 aa 200-300 conjugated to Keyhole Limpet Haemocyanin.
pH: 7.4
Preservative: 0.02% Proclin 300
Constituents: 50% Glycerol (glycerin, glycerine), 48.98% TBS, 1X, 1% BSA
IHC-P | |
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Human | Predicted |
Mouse | Predicted |
Rat | Tested |
Species | Dilution info | Notes |
---|---|---|
Species Rat | Dilution info 1/100.00000 - 1/500.00000 | Notes When using a fluorescent probe the recommended dilution is 1/50 – 1/200. |
Species | Dilution info | Notes |
---|---|---|
Species Mouse, Human | Dilution info - | Notes - |
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A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed:10681376, PubMed:11555828, PubMed:12865317, PubMed:19965576, PubMed:9435160). 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:10681376, PubMed:11555828, PubMed:12865317, PubMed:19965576, PubMed:9435160). Catalyzes the hydroxylation of carbon-hydrogen bonds (PubMed:11555828, PubMed:12865317). Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2 (PubMed:11555828, PubMed:12865317). Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis (PubMed:21576599). May act as a major enzyme for all-trans retinoic acid biosynthesis in the liver. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid (PubMed:10681376). Primarily catalyzes stereoselective epoxidation of the last double bond of polyunsaturated fatty acids (PUFA), displaying a strong preference for the (R,S) stereoisomer (PubMed:19965576). Catalyzes bisallylic hydroxylation and omega-1 hydroxylation of PUFA (PubMed:9435160). May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent) (PubMed:21068195). Plays a role in the oxidative metabolism of xenobiotics. Catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin (PubMed:14725854). Metabolizes caffeine via N3-demethylation (Probable).
Cytochrome P450 1A2, CYPIA2, Cholesterol 25-hydroxylase, Cytochrome P(3)450, Cytochrome P450 4, Cytochrome P450-P3, Hydroperoxy icosatetraenoate dehydratase, CYP1A2
Rabbit Polyclonal Cytochrome P450 1A2 antibody. Suitable for IHC-P and reacts with Rat samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human CYP1A2 aa 200-300 conjugated to Keyhole Limpet Haemocyanin.
pH: 7.4
Preservative: 0.02% Proclin 300
Constituents: 50% Glycerol (glycerin, glycerine), 48.98% TBS, 1X, 1% BSA
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Cytochrome P450 1A2 often known as CYP1A2 is an important enzyme in the cytochrome P450 superfamily with a known mass around 58 kDa. It is mainly expressed in the liver where it functions in the metabolism of drugs and the bioactivation of various compounds. CYP1A2 also participates in the oxidation of small organic molecules which include xenobiotics and endogenous substrates. Due to its function researchers frequently study CYP1A2 substrates and its inhibitors to understand better its role in drug metabolism and toxicity.
CYP1A2 plays a central role in the oxidative biotransformation of drugs and procarcinogens. It does not form part of a larger complex but interacts dynamically with other enzymes in the detoxification process. CYP1A2 metabolizes several clinical drugs such as caffeine and theophylline and regulates the detoxification of aromatic amines and hydrocarbons. Studying CYP1A2 inhibitors can provide insights into clinically relevant drug interactions and potential side effects in pharmacotherapy.
CYP1A2 functions within the drug metabolism and synthesis of cholesterol steroids and other lipids pathways. In the drug metabolism pathway CYP1A2 works alongside other cytochrome P450 enzymes such as CYP1A1 and CYP1B1 which together ensure the metabolism and clearance of various exogenous and endogenous compounds. These pathways are vital for maintaining drug efficacy and preventing toxicity through the metabolic clearance of pharmaceutical agents and harmful substances.
CYP1A2 activity links to liver disorders and certain cancers. Altered enzyme activity may lead to hepatotoxicity a condition that arises from excessive accumulation of active drug metabolites in the liver. Furthermore due to its role in activating procarcinogens increased CYP1A2 activity relates to a higher risk of developing certain cancers including liver cancer. Researchers often explore these connections to better understand the enzyme's role in disease pathogenesis and to develop CYP1A2-directed therapies.
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Immunohistochemical analysis of formalin-fixed and paraffin-embedded rat liver tissue labeling Cytochrome P450 1A2 with ab217377 at 1/200 dilution followed by conjugation to the secondary antibody and DAB staining.
Immunohistochemical analysis of formalin-fixed and paraffin-embedded rat liver tissue labeling Cytochrome P450 1A2 with ab217377 at 1/200 dilution followed by conjugation to the secondary antibody and DAPI staining.
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