Entrop et al. published in Cell Death & Disease

Kristin Entrop, Senait Wieske & Markus Rehm 

During apoptosis signaling, Bcl-2-associated X protein (Bax) translocates from the cytosol to the mitochondria to form pores in their outer membrane, allowing for the release of intermembrane proteins into the cytosol and thereby triggering apoptosis execution. Since its discovery in 1993 [1], Bax is, therefore, one of the most widely studied regulators of programmed cell death (>45,000 publications are returned on the search string “(Bax) AND (apoptosis)” on pubmed at the time of writing), with numerous studies investigating (changes in) expression amounts and localization of Bax in various scenarios of cellular stress conditions and in models for proliferative and degenerative diseases, using antibody-based assays. In contrast to comprehensively authenticated antibodies for clinical diagnostics, the sensitivity and specificity of antibody-based detections used in basic research are often far less thoroughly assessed by commercial suppliers for routine applications such as immunoblotting and immunofluorescence-based detection. One of the most widely used antibodies for Bax detection is a mouse monoclonal antibody raised against amino acids 1–171 of mouse Bax and with supposed reactivity to Bax of mouse, rat and human origin, available from Santa Cruz Biotechnology Inc. (Bax Antibody (B-9): sc-7480; https://www.scbt.com/p/bax-antibody-b-9). The use of this antibody, according to the manufacturer’s information, has been documented in >1400 scientific publications so far (see Supplementary Information 1 for a list valid as of May 2024).