Bag-2 Background Information Bag-2 (Bcl-2-associated athanogene 2), also known as Bag family molecular chaperone regulator 2, is a member of the Bag family of proteins and contains the most diverged of the characteristic C-terminal Bag domain. Via their Bag domain, Bag proteins bind with high affinity to the HSC 70/HSP 70 ATPase domain, regulating chaperone activity and apoptosis. Bag-2 is an evolutionarily conserved cytoplasmic protein with putative N-terminal phosphorylation sites and specifically functions as an HSC 70 co-chaperone. Bag-2 is a major component of the HSC 70/CHIP chaperone-dependent ubiquitin ligase complex and acts to disrupt CHIP-mediated ubiquitylation. In this complex, Bag-2 directly interacts with the ATPase domain of HSC 70 as well as the U-box domain of CHIP and inhibits ubiquitylation by interfering with the association between CHIP and its ubiquitin conjugating enzyme.
Bag-2 (A-12)
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Bag-2 (A-12): sc-101216. Western blot analysis of Bag-2 expression in HeLa whole cell lysate.
Bag-2 (A-12): sc-101216. Western blot analysis of Bag-2 expression in non-transfected 293: sc-110760 (A), human Bag-2 transfected 293: sc-128081 (B) and HeLa (C) whole cell lysates.
