| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:2000 |
| IHC | 1:50-1:200 |
ATG7 serves as a critical E1-like activating enzyme in the autophagy pathway, functioning as an essential regulator of both ATG12 and LC3 conjugation systems. This dual role positions ATG7 at the heart of autophagosome formation, making it an indispensable marker for researchers investigating cellular quality control mechanisms, stress responses, and the increasingly recognized connections between autophagy dysregulation and disease states including cancer and neurodegeneration.
This recombinant monoclonal antibody, clone 15C7, offers the reproducibility that autophagy research demands. Generated through recombinant technology with a defined sequence, it eliminates the lot-to-lot variability that can complicate longitudinal studies or multi-site collaborations. The rabbit host and monoclonal nature ensure consistent epitope recognition against the immunizing peptide derived from human ATG7.
Validation data demonstrates reliable performance across multiple experimental platforms. In western blot applications, the antibody detects ATG7 at the expected 78 kDa molecular weight across diverse human cell lines including K562, Jurkat, HeLa, and THP-1, confirming robust detection in both suspension and adherent cell models at dilutions ranging from 1:500 to 1:2000. For tissue-based studies, immunohistochemistry validation in paraffin-embedded human colorectal cancer tissue shows clear staining at 1:100 dilution using standard citrate-based antigen retrieval, providing researchers with a validated protocol for examining ATG7 expression in clinical specimens.
The unconjugated format and affinity-purified preparation offer flexibility for downstream detection strategies. Whether investigating basal autophagy levels, monitoring pathway activation under stress conditions, or characterizing ATG7 expression patterns in tumor samples, this antibody provides a dependable tool for advancing understanding of this fundamental cellular process.
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