The ALDH1A2 antibody is a polyclonal antibody that detects endogenous human ALDH1A2. ALDH1A2 (also known as RALDH) is an enzyme belonging to the aldehyde dehydrogenase family. The protein encoded by this gene catalyzes the irreversible oxidation of retinaldehyde to form retinoic acid (RA). RA is an important hormone that regulates cell growth, differentiation, and apoptosis under both physiological and pathological conditions.

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Mutations in this gene have been associated with a variety of neurological diseases including schizophrenia, Alzheimer’s disease, and Parkinson’s disease. The enzyme also plays an essential role in adipose tissue metabolism by converting glycerol 3-phosphate to acetaldehyde, which is then converted to ethanol in the liver. A single base pair mutation in ALDH2 (Glu487 to Lys487), common in East Asians, results in defective alcohol dehydrogenase and leads to the facial flushing syndrome when these individuals consume alcoholic beverages.

Previous studies have shown that low ALDH1A2 expression correlates with poor prognosis in HNSCC patients and that its downregulation is a result of gene promoter hypermethylation. We showed that a high level of ALDH1A2 expression is required for effective RA-dependent antitumor effects of natural and synthetic retinoids in tumor cells and mouse models. Our data further support the hypothesis that reduced ALDH1A2 activity and/or function contributes to treatment failure in a subset of OPSCC patients and may serve as an attractive biomarker to stratify patients for whom a combination of conventional and chemotherapeutic agents might be beneficial. Furthermore, we demonstrate that the radiosensitization of Cal27 tumor cells by a combination of ATRA and irradiation is accompanied by a concentration-dependent increase in cleaved caspase 3 levels, indicative of accelerated apoptosis.