Recombinant Human BAG family molecular chaperone regulator 3 (BAG3)

Uniprot Id

O95817

Target Species

Human

Target Name

BAG3

Target Full Name

BAG family molecular chaperone regulator 3

Target Function

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 HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70. Has anti-apoptotic activity. Plays a role in the HSF1 nucleocytoplasmic transport.

Target Involvement

Myopathy, myofibrillar, 6 (MFM6); Cardiomyopathy, dilated 1HH (CMD1HH)

Target Subcellular Location

Nucleus. Cytoplasm.

Target Synonyms

BAG 3; BAG family molecular chaperone regulator 3; BAG-3; Bag3; BAG3_HUMAN; Bcl 2 binding protein; Bcl-2-associated athanogene 3; Bcl-2-binding protein Bis; BCL2 associated athanogene 3; BCL2 binding athanogene 3; BIS; CAIR 1; Docking protein CAIR 1; Docking protein CAIR-1; MFM6

Target Background

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.