Cat. #152158
Anti-Cytochrome P450 2A6 [RP1.2B4]
Cat. #: 152158
Sub-type: Primary antibody
Unit size: 100 ug
Availability: 10-12 weeks
Target: Cytochrome P450 2A6, CYP2A6
Class: Monoclonal
Application: WB
Reactivity: Human
Host: Mouse
£300.00
This fee is applicable only for non-profit organisations. If you are a for-profit organisation or a researcher working on commercially-sponsored academic research, you will need to contact our licensing team for a commercial use license.
Contributor
Inventor: Ayham Alnabulsi
Institute: Vertebrate Antibodies Limited
Tool Details
*FOR RESEARCH USE ONLY
- Name: Anti-Cytochrome P450 2A6 [RP1.2B4]
- Clone: RP1.2B4
- Tool sub type: Primary antibody
- Class: Monoclonal
- Conjugation: Unconjugated
- Strain: Balb/c
- Reactivity: Human
- Host: Mouse
- Application: WB
- Description: Exhibits a high coumarin 7-hydroxylase activity. Can act in the hydroxylation of the anti-cancer drugs cyclophosphamide and ifosphamide. Competent in the metabolic activation of aflatoxin B1. Constitutes the major nicotine C-oxidase. Possesses low phenacetin O-deethylation activity.
- Immunogen: Human cytochrome P450 CYP2A6
- Isotype: IgG1 kappa
- Myeloma used: P3X63Ag8.653
- Recommended controls: western blot: Recombinant P450 - 0.49 pmol per lane.
Target Details
- Target: Cytochrome P450 2A6, CYP2A6
- Tissue cell line specificity: western blot: Recombinant P450 - 0.49 pmol per lane.
- Target background: Exhibits a high coumarin 7-hydroxylase activity. Can act in the hydroxylation of the anti-cancer drugs cyclophosphamide and ifosphamide. Competent in the metabolic activation of aflatoxin B1. Constitutes the major nicotine C-oxidase. Possesses low phenacetin O-deethylation activity.
Applications
- Application: WB
Handling
- Format: Liquid
- Concentration: 0.9-1.1 mg/ml
- Unit size: 100 ug
- Storage buffer: PBS with 0.02% azide
- Storage conditions: -15° C to -25° C
- Shipping conditions: Shipping at 4° C
References
- Barnes, T. S. (1987). The generation and characterization of monoclonal antibodies to human cytochrome P450. Ph. D. Thesis. University of Aberdeen.
