| Code | CSB-RA441570A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| FC | 1:50-1:200 |
ATG9A serves as the only multi-spanning transmembrane protein in the core autophagy machinery, playing an essential role in autophagosome formation by delivering membrane to expanding phagophores. This unique trafficking protein cycles between the trans-Golgi network and endosomes, making it a critical marker for researchers investigating autophagy initiation, membrane dynamics, and cellular stress responses.
This recombinant monoclonal antibody, clone 7G12, 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 IgG format, raised against a synthetic peptide derived from human ATG9A, provides consistent performance across your experimental timeline.
Validation in flow cytometry demonstrates clear detection of ATG9A in HepG2 human hepatocellular carcinoma cells. Using fixed and permeabilized cells with a 1:100 dilution, the antibody produces a distinct positive shift compared to isotype control, confirming reliable intracellular staining. This hepatocyte-derived cell line represents a particularly relevant model given the liver's high autophagic activity and the importance of autophagy in hepatic metabolism and disease. The validated protocol, employing 4% formaldehyde fixation and 0.2% Triton X-100 permeabilization, provides a solid starting point for your own flow cytometry workflows, with recommended dilutions ranging from 1:50 to 1:200 allowing optimization flexibility.
Whether you are characterizing autophagy flux, investigating ATG9A trafficking patterns, or exploring connections between autophagy and metabolic disease, this antibody supports quantitative single-cell analysis through flow cytometry and detection via ELISA, enabling diverse experimental approaches to study this fundamental cellular pathway.
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