Western blot analysis of BAG2. Using BAG2 polyclonal antibody (Cat # PAB0329) at 1 : 2000. HeLa stably transfected Myc-tagged CHIP (carboxyl terminus of Hsp70-interacting protein) were immunoprecipitated with an anti-Myc antibody. Immunocomplexes were resolved by SDS-PAGE followed by western blot analysis of BAG2. This experiment was done to show the colocalization of CHIP and Bag2. Please refer to Dai et al (2005) for additional information on HeLa cells stably transfected with Myc-CHIP.
Immunofluorescence confocal microscopy of BAG2. Using BAG2 polyclonal antibody (Cat # PAB0329) at 1 : 2000. HeLa cells stably transfected with Myc-CHIP (carboxyl terminus of Hsp70-interacting protein) and growing on coverslips were left untreated (A) or heat shocked at 42 degrees for 30 min (B) . Cells were fixed with 3.7% paraformaldehyde, permeabilized with 0.5% Triton X-100 prior to antibody staining. BAG2 localized to the cytoplasm of untreated cells, and to the nucleus of cells subjected to heat shock. Please refer to Dai et al (2005) for additional information on HeLa cells stably transfected with Myc-CHIP.
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 predicted BAG2 protein contains 211 amino acids. 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