BAX (the BCL-2-associated X protein), a cardinal pro-apoptotic member of the BCL-2 family, is a latent, cytosolic and monomeric protein that plays an important role in the mitochondria-dependent apoptotic pathway. The nuclear magnetic resonance (NMR) spectroscopic analysis suggests that the structure of Bax consists of nine α-helices (α1 to α9) connected by short loops, in which α5, α6 and α9 are involved in the interaction of Bax with outer mitochondrial membrane (OMM). Bax remains inactive in cytosol and goes through conformational changes triggered by a cell death signal to insert, oligomerize and form large pores through the OMM with the releasing of different apoptogenic factors.
- A4484 PRIMA-1METSummary: Restore mutant p53 activity, induce BAX and PUMA
- A4483 PRIMA-1Target: p53Summary: BAX inhibitor
- A4462 Bax inhibitor peptide, negative controlSummary: Peptide inhibit Bax translocation to mitochondria
- A4461 Bax inhibitor peptide V5Target: BaxSummary: Bax inhibitor
- A4460 Bax inhibitor peptide P5Summary: Bax inhibitor
- A4459 Bax channel blockerSummary: Inhibitor of Bax-mediated mitochondrial cytochrome c release
- A3218 BAM7Summary: BAX activator,direct and selective