Anti-CYP2B6 monoclonal antibody (DCABH-3785)

Specifications


Host Species
Rabbit
Antibody Isotype
IgG
Clone
FQS0096(C)
Species Reactivity
Human
Immunogen
Synthetic peptide (the amino acid sequence is considered to be commercially sensitive)
Conjugate
Unconjugated

Applications


Application Notes
WB: 1/1000 - 1/10000.
*Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own experiment using appropriate negative and positive controls.

Target


Alternative Names
CYP2B6; cytochrome P450, family 2, subfamily B, polypeptide 6; CYP2B, cytochrome P450, family 2, subfamily B , cytochrome P450, subfamily IIB (phenobarbital inducible) , cytochrome P450, subfamily IIB (phenobarbital inducible), polypeptide 6; cytochrom
Entrez Gene ID
UniProt ID

Product Background


Gene summary
CYP2B6 (Cytochrome P450 Family 2 Subfamily B Member 6) is a Protein Coding gene. Diseases associated with CYP2B6 include efavirenz, poor metabolism of and cyp2b6-related altered drug metabolism. Among its related pathways are Metabolism and cytochrome P450. GO annotations related to this gene include iron ion binding and oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen. An important paralog of this gene is CYP2C19. This gene, CYP2B6, 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 its expression is induced by phenobarbital. The enzyme is known to metabolize some xenobiotics, such as the anti-cancer drugs cyclophosphamide and ifosphamide. Transcript variants for this gene have been described; however, it has not been resolved whether these transcripts are in fact produced by this gene or by a closely related pseudogene, CYP2B7. Both the gene and the pseudogene are located in the middle of a CYP2A pseudogene found in a large cluster of cytochrome P450 genes from the CYP2A, CYP2B and CYP2F subfamilies on chromosome 19q.
Antigen Description
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,4-cineole 2-exo-monooxygenase. Cytochrome P450 2B6 is an enzyme that in humans is encoded by the CYP2B6 gene. CYP2B6 is a member of the Cytochrome P450 group of enzymes. Along with CYP2A6, it is involved with metabolizing nicotine, along with many other substances. This gene, CYP2B6, 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 its expression is induced by phenobarbital. The enzyme is known to metabolize some xenobiotics, such as the anti-cancer drugs cyclophosphamide and ifosphamide. The function about CYP2B6 antigen include aromatase activity; electron carrier activity; heme binding; metal ion binding; monooxygenase activity.
Pathway
Arachidonic acid metabolism, organism-specific biosystem; Arachidonic acid metabolism, conserved biosystem; Biological oxidations, organism-specific biosystem; Cytochrome P45 - arranged by substrate type, organism-specific biosystem; Drug metabolism - cytochrome P45, organism-specific biosystem; Drug metabolism - cytochrome P45, conserved biosystem; Metabolic pathways, organism-specific biosystem.

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References


Kazui, M; Nishiya, Y; et al. Identification of the Human Cytochrome P450 Enzymes Involved in the Two Oxidative Steps in the Bioactivation of Clopidogrel to Its Pharmacologically Active Metabolite. DRUG METABOLISM AND DISPOSITION 38:92-99(2010).
Lewis, DFV; Lake, BG; et al. Molecular modelling of mammalian CYP2B isoforms and their interaction with substrates, inhibitors and redox partners. XENOBIOTICA 27:443-478(1997).

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