CYP2D6 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 1
- PROTOCOLS
- BACKGROUND
Application
| IHC-P, WB, E |
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Primary Accession | P10635 |
Other Accession | P12939, P10633 |
Reactivity | Human |
Predicted | Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 55769 Da |
Antigen Region | 76-105 aa |
Gene ID | 1565 |
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Other Names | Cytochrome P450 2D6, CYPIID6, Cytochrome P450-DB1, Debrisoquine 4-hydroxylase, CYP2D6, CYP2DL1 |
Target/Specificity | This CYP2D6 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 76-105 amino acids from the N-terminal region of human CYP2D6. |
Dilution | WB~~1:1000 IHC-P~~1:10~50 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | CYP2D6 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | CYP2D6 {ECO:0000303|PubMed:21289075, ECO:0000312|HGNC:HGNC:2625} |
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Function | A cytochrome P450 monooxygenase involved in the metabolism of fatty acids, steroids and retinoids (PubMed:18698000, PubMed:19965576, PubMed:20972997, PubMed:21289075, 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:18698000, PubMed:19965576, PubMed:20972997, PubMed:21289075, PubMed:21576599). Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA) (PubMed:19965576, PubMed:20972997). Metabolizes endocannabinoid arachidonoylethanolamide (anandamide) to 20-hydroxyeicosatetraenoic acid ethanolamide (20-HETE-EA) and 8,9-, 11,12-, and 14,15-epoxyeicosatrienoic acid ethanolamides (EpETrE-EAs), potentially modulating endocannabinoid system signaling (PubMed:18698000, PubMed:21289075). Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes cholesterol toward 25- hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis (PubMed:21576599). Catalyzes the oxidative transformations of all-trans retinol to all-trans retinal, a precursor for the active form all-trans-retinoic acid (PubMed:10681376). Also involved in the oxidative metabolism of drugs such as antiarrhythmics, adrenoceptor antagonists, and tricyclic antidepressants. |
Cellular Location | Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein |
Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum and is known to metabolize as many as 20% of commonly prescribed drugs. Its substrates include debrisoquine, an adrenergic-blocking drug; sparteine and propafenone, both anti-arrythmic drugs; and amitryptiline, an anti-depressant. The gene is highly polymorphic in the population; certain alleles result in the poor metabolizer phenotype, characterized by a decreased ability to metabolize the enzyme's substrates. The gene is located near two cytochrome P450 pseudogenes on chromosome 22q13.1. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
References
Abduljalil, K., et al. Clin. Pharmacol. Ther. 88(5):643-651(2010)
Novalbos, J., et al. J Clin Psychopharmacol 30(5):504-511(2010)
Thompson, A.M., et al. Breast Cancer Res. Treat. (2010) In press :
Gonzalez-Tejera, G., et al. P R Health Sci J 29(3):299-304(2010)
Abraham, J.E., et al. Breast Cancer Res. 12 (4), R64 (2010) :
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