BAG Family Molecular Chaperone Regulator 3 (BAG3) Human Recombinant Protein

BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The protein encoded by this gene contains a WW domain in the N-terminal region and a BAG domain in the C-terminal region. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner. [provided by RefSeq, Jul 2008]

BAG3: a co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSC70. Has anti-apoptotic activity. Plays a role in the HSF1 nucleocytoplasmic transport. May be involved in neuronal differentiation and migration.

Protein type: Apoptosis; Chaperone

Chromosomal Location of Human Ortholog: 10q26.11

Cellular Component: cell-cell adherens junction; cytoplasm; cytosol; plasma membrane

Molecular Function: adenyl-nucleotide exchange factor activity; protein binding

Biological Process: induction of apoptosis via death domain receptors

Disease: Cardiomyopathy, Dilated, 1hh; Myopathy, Myofibrillar, 6