Bag-5 Background Information Bag-5 (Bcl-2-associated athanogene 5), also known as Bag family molecular chaperone regulator 5, is a member of the Bag family of proteins and contains four Bag domains. Via their Bag domain, Bag proteins bind with high affinity to the HSC 70/HSP 70 ATPase domain, regulating chaperone activity and apoptosis. Bag-5 is a component of the HSP 70/Parkin complex and acts to inhibit Parkin E3 ubiquitin ligase activity and HSP 70 chaperone activity. In this complex, Bag-5 directly interacts with the ATPase domain of HSP 70 and the N-terminal linker region of Parkin. Bag-5 expression is induced upon dopaminergic neuron injury and functions to sensitize the neurons to injury-induced cell death. In addition, Bag-5 may be a useful target in therapies for neurodegenerative diseases such as Parkinson’s disease which is caused by a mutation in the gene encoding Parkin.
Bag-5 (18Z)
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Bag-5 (18Z): sc-101215. Western blot analysis of Bag-5 expression in Jurkat whole cell lysate.
Bag-5 (18Z): sc-101215. Western blot analysis of Bag-5 expression in non-transfected: sc-117752 (A) and mouse Bag-5 transfected: sc-118669 (B) 293T whole cell lysates.