Bag-2 (L-21) 抗体: sc-130969

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.