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Recombinant Anti-Cytochrome P450 1A2 Rabbit mAb

Western blot analysis of Cytochrome P450 1A2 expression in Caco2 (A) whole cell lysates. (Predicted band size: 58 kD; Observed band size: 52 kD)
Immunofluorescent analysis of Cytochrome P450 1A2 staining in Caco2 cells. Formalin-fixed cells were permeabilized with 0.1% Triton X-100 in TBS for 5-10 minutes and blocked with 3% BSA-PBS for 30 minutes at room temperature. Cells were probed with the primary antibody in 3% BSA-PBS and incubated overnight at 4 °C in a hidified chamber. Cells were washed with PBST and incubated with an AF488-conjugated secondary antibody (green) in PBS at room temperature in the dark. Phalloidin - AF594 was used to stain Actin filaments (red). DAPI was used to stain the cell nuclei (blue).

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Product Information
Application Applications Legend: E=ELISA WB=Western Blotting IHC=Immunohistochemistry IHC-P=Immunohistochemistry (Paraffin) IP=Immunoprecipitation IF=Immunofluorescence IC=Immunochemistry ICC=Immunocytochemistry FC=Flow Cytometry DB=Dot Blot	WB, FC, IF/IC
Primary Accession	P05177
Reactivity	Human
Host	Rabbit
Clonality	Monoclonal
Calculated MW	58407 Da

Additional Information
Gene ID	1544
Other Names	Cytochrome P450 1A2; CYPIA2; Cytochrome P(3)450; Cytochrome P450 4; Cytochrome P450-P3
Target/Specificity	KLH-conjugated synthetic peptide encompassing a sequence within human Cytochrome P450 1A2 protein. The exact sequence is proprietary.
Dilution	WB~~WB (1/500 - 1/1000) FC~~1:10~50 IF/IC~~N/A
Format	Liquid in PBS, pH 7.3, 50% glycerol, 0.05% BSA, and 0.05% Proclin300.
Storage	Store at -20 °C.Stable for 12 months from date of receipt

For Research Use Only. Not For Use In Diagnostic Procedures.

Protein Information
Name	CYP1A2 {ECO:0000303\|PubMed:2575218, ECO:0000312\|HGNC:HGNC:2596}
Function	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).
Cellular Location	Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein
Tissue Location	Liver.