Use of Glyceraldehyde 3-Phosphate Dehydrogenase (GAPDH) as Internal Control in Western-Blot Experiments?

Abstract

to 1, 3-biphosphoglycerate during glycolysis, GAPDH is involved in several non-metabolic processes, including transcriptional activation and cell apoptosis [3]. Activated Akt2 may increase ovarian cancer cell survival via prevention of GAPDH-induced apoptosis. This effect of Akt2 is partially mediated by its phosphorylation of GAPDH at Thr-237, which results in the prevention of GAPDH nuclear translocation [3]. This study prove that GAPDH is S-nitrosylated by Nitric Oxide (NO) in response to cell stress, which result in, it to bind the protein Siah1, anubiquitin ligase. The complex moves into the nucleus where Siah1 targets nuclear proteins for degradation, thus beginning controlled cell shutdown [4].