| Code | CSB-RA178519A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:5000 |
| IHC | 1:50-1:200 |
Cytochrome P450 1A2 plays a central role in hepatic drug metabolism, catalyzing the oxidation of numerous xenobiotics, pharmaceuticals, and endogenous compounds. As a key enzyme in phase I metabolism, CYP1A2 influences the pharmacokinetics of clinically important drugs and participates in the bioactivation of procarcinogens, making it an essential target for researchers investigating drug-drug interactions, toxicology, and cancer susceptibility.
This recombinant monoclonal antibody offers the reproducibility that demanding experimental workflows require. Generated through recombinant technology with a defined sequence, it eliminates the lot-to-lot variability inherent to traditional hybridoma-derived antibodies, ensuring consistent performance across long-term studies and multi-site collaborations. The rabbit IgG format, produced against a synthetic peptide derived from human Cytochrome P450 1A2, provides high specificity for your target.
Validation studies confirm robust performance across multiple applications. In western blot analysis, the antibody detects a band at the predicted molecular weight of 59 kDa in HeLa, HepG2, and L02 whole cell lysates, with effective dilutions ranging from 1:500 to 1:5000 offering flexibility to optimize signal intensity for your specific experimental conditions. For tissue-based studies, immunohistochemistry validation in paraffin-embedded human kidney tissue demonstrates clear staining at 1:50 to 1:200 dilutions using standard citrate buffer antigen retrieval, providing a reliable option for examining CYP1A2 expression patterns in clinical and research specimens.
Whether you are exploring metabolic enzyme regulation, investigating drug metabolism pathways, or examining CYP1A2 expression in cancer and cardiovascular disease contexts, this antibody delivers the consistency and validated performance needed to advance your research with confidence.
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