Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting
Background: Angiomotin (AMOT) is a widely expressed cell junction protein initially identified through its ability to bind angiostatin. Alternative splicing results in two isoforms of angiomotin, the full-length p130 and the amino-terminally truncated p80. These isoforms, along with angiomotin-like 1 (AmotL1) and angiomotin-like 2 (AmotL2) comprise the Motin protein family. Angiomotin is important in endothelial cell polarity, migration and blood vessel formation during development, as well as in signaling through small GTPases and the Hippo/YAP pathway (reviewed in 1).Research studies have shown that angiomotin expression regulates migration and proliferation of breast cancer cells (2,3).
Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting
Background: The ATPase inhibitor factor 1 (ATPIF1) gene encodes a mitochondrial ATPase inhibitor that limits ATP depletion when mitochondrial respiration is impaired (1). ATPIF1 becomes activated following a drop in pH, binding to β-F1-ATPase, thereby inhibiting the hydrolase activity of the H+-ATP synthase (1,2). In addition to its role as an ATP hydrolase, ATPIF1 has also been shown to play a regulatory role in cellular energy metabolism by triggering the induction of aerobic glycolysis in cancer cells resulting in their Warburg phenotype (3,4). Research studies demonstrate that the overexpression of ATPIF1 in several human carcinomas further supports its participation in oncogenesis and provides insight into the altered metabolism of cancer cells, which includes the reprogramming of energetic metabolism toward glycolysis (3).