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.

推荐稀释比 WB: 1/1000-1/5000; FC: 1/200-1/2000; ICC/IF: 1/100-1/1000

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Flow cytometric analysis of BAG cochaperone 3 expression in HepG2 cells using BAG cochaperone 3 antibody . Green, isotype control; red, BAG cochaperone 3.

Immunocytochemical staining of HepG2 cells with BAG cochaperone 3 antibody . Nuclei were stained blue with DAPI; BAG cochaperone 3 was stained magenta with Alexa Fluor® 647. Images were taken using Leica stellaris 5. Protein abundance based on laser Intensity and smart gain: Medium. Scale bar, 20 μm.

Western blotting analysis using BAG cochaperone 3 antibody . Total cell lysates (30 μg) from various cell lines were loaded and separated by SDS-PAGE. The blot was incubated with BAG cochaperone 3 antibody and HRP-conjugated goat anti-rabbit secondary antibody respectively. Image was developed using FeQ™ ECL Substrate Kit .

Western blotting analysis using BAG cochaperone 3 antibody . BAG cochaperone 3 expression in wild type (WT) and BAG cochaperone 3 shRNA knockdown (KD) Hela cells with 30 μg of total cell lysates. β-Tubulin serves as a loading control. The blot was incubated with BAG cochaperone 3 antibody and HRP-conjugated goat anti-rabbit secondary antibody respectively. Image was developed using FeQ™ ECL Substrate Kit .

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