A number of cellular and animal models recapitulate key aspects of prostate cancer progression, including a decreased or loss of ALDH1A2 expression and altered retinoid metabolism and signaling. Moreover, a reduction in ALDH1A2 activity is observed in the human prostate microenvironment and correlates with reduced sensitivity to retinoids.
The ALDH1A2 antibody production of the ALDH family are cytosolic enzymes that catalyze the oxidative decarboxylation of many different aromatic compounds. They are highly conserved tetramers with three domains (catalytic, cofactor binding, and oligomerization) that form a funnel-like structure for the binding of NAD+ and aldehyde substrate [1, 26]. The active site is accessible only through a region within the cofactor binding domain. The specificity of ALDHs for various aldehydes is determined by the residues lining this funnel. The presence of divalent metal cations, such as Mg2+ and Ca2+, enhances enzyme activity by stabilizing the cofactor binding domain and improving access to the active site.
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In human prostate epithelial cells, ALDH1A2 is expressed predominantly in the luminal cell population but also in basal cells. Its overexpression is correlated with poor prognosis in human prostate cancer. Aldh1A2 overexpression has been observed in a subset of patients with gastric cancer and a number of other malignancies.
We have produced a rabbit polyclonal antibody that specifically recognizes the mouse ALDH1A2 isoform. The antibody demonstrates very low cross-reactivity with the other members of the ALDH family and does not cross-react with human ALDH1A1. This protein can be used for immunoblot analysis on whole cell extracts from TRAMP mice or in vitro assays.…