| Code | CSB-RA999377A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:5000 |
| IHC | 1:50-1:200 |
Monoamine oxidase B is a mitochondrial outer membrane enzyme that catalyzes the oxidative deamination of biogenic and xenobiotic amines, playing a central role in neurotransmitter metabolism and cellular redox homeostasis. MAOB activity has garnered significant research attention due to its involvement in neurodegenerative conditions, where elevated expression contributes to oxidative stress and neuronal damage. Beyond neuroscience, MAOB expression patterns in hepatic and tumor tissues make it a relevant target for cancer metabolism studies and therapeutic development.
This recombinant monoclonal antibody, generated from clone 9B6 in rabbit host, offers the reproducibility and batch consistency that demanding experimental workflows require. Because the antibody sequence is defined and produced recombinantly, researchers can expect uniform performance across studies, eliminating the lot-to-lot variability that can complicate long-term projects or multi-site collaborations. The antibody was raised against a synthetic peptide derived from human Monoamine Oxidase B, ensuring precise epitope targeting.
Validation studies demonstrate reliable performance across multiple applications. Western blot analysis detects MAOB at the expected 59 kDa molecular weight in both L02 and HepG2 whole cell lysates, with effective dilutions ranging from 1:500 to 1:5000. For tissue-based investigations, immunohistochemistry has been validated in paraffin-embedded human liver and brain sections at 1:50 to 1:200 dilutions using citrate buffer antigen retrieval, producing clear staining patterns consistent with known MAOB distribution in these metabolically active tissues.
Whether investigating dopaminergic pathway regulation, characterizing tumor metabolic phenotypes, or exploring MAOB as a therapeutic target, this antibody provides the specificity and consistency needed for rigorous experimental design.
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