BAG3 (E7Y9T) Rabbit Monoclonal Antibody#23842,Cell Signaling Technology (CST),23842

BCL2-associated athanogene 3 (BAG3) is a member of the BAG domain-containing family of proteins important for protein homeostasis, including trafficking of misfolded proteins and the regulation of molecular chaperones, transcription factors, and autophagy (1-3). BAG3 is closely associated with molecular chaperones by interacting with the N-terminal ATPase domain of 70 kDa heat shock protein (HSP70) (4). HSP70 is a highly versatile molecular chaperone that is regulated by environmental stresses and interacts with unfolded proteins to promote proper refolding and prevent irreversible aggregation (5). BAG3 function has been associated with the regulation of apoptotic proteins and targeting polyubiquitinated client proteins for autophagic degradation (2). Expression of BAG3 is elevated in a variety of tumor types and regulates multiple aspects of cancer progression including cell adhesion, metastasis, angiogenesis, enhanced autophagic activity, and inhibition of apoptosis (2).Sherman, M.Y. and Gabai, V. (2022)J Cell Biochem123, 43-53.Kögel, D. et al. (2020) Cells 9, 574-590.Klimek, C. et al. (2017)J Cell Sci130, 2781-2788.Takayama, S. et al. (1999)J Biol Chem274, 781-6.Nollen, E.A. and Morimoto, R.I. (2002)J Cell Sci115, 2809-16.Alternate NamesBAG cochaperone 3; BAG family molecular chaperone regulator 3; BAG-3; BAG-family molecular chaperone regulator-3; BAG3; Bcl-2-associated athanogene 3; Bcl-2-binding protein Bis; BCL2 associated athanogene 3; BCL2-associated athanogene 3; BCL2-binding athanogene 3; BIS; CAIR-1; Docking protein CAIR-1; MFM6; MGC104307

BAG cochaperone 3; BAG family molecular chaperone regulator 3; BAG-3; BAG-family molecular chaperone regulator-3; BAG3; Bcl-2-associated athanogene 3; Bcl-2-binding protein Bis; BCL2 associated athanogene 3; BCL2-associated athanogene 3; BCL2-binding athanogene 3; BIS; CAIR-1; Docking protein CAIR-1; MFM6; MGC104307