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Antibody detects endogenous levels of BAG3 only when phosphorylated at Tyr457.
BAG3 are among BAG proteins that 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.
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Protein Aliases: BAG family molecular chaperone regulator 3; BAG-3; Bcl-2-associated athanogene 3; Bcl-2-binding protein Bis; Bcl-2-interacting death suppressor; BCL2-associated athanogene 3; BCL2-binding athanogene 3; DKFZp434E0610; Docking protein CAIR-1; MGC104307
Gene Aliases: AA407278; BAG-3; BAG3; BIS; CAIR-1; MFM6; mg638; MNCb-2243
UniProt ID: (Human) O95817, (Mouse) Q9JLV1
Entrez Gene ID: (Human) 9531, (Mouse) 29810, (Rat) 293524
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