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BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. Additionally we are shipping BAG3 Antibodies (93) and BAG3 Kits (12) and many more products for this protein.
Showing 10 out of 14 products:
Human BAG3 Protein expressed in Escherichia coli (E. coli) - ABIN667755
Kyratsous, Silverstein: The co-chaperone BAG3 regulates Herpes Simplex Virus replication. in Proceedings of the National Academy of Sciences of the United States of America 2008
Show all 2 references for ABIN667755
Human BAG3 Protein expressed in Wheat germ - ABIN1346366
Chen, Yang, Cheng, Tu, Guo, Le, Xiong, Mo, Li, Jeong, Jiang, Blackshaw, Bi, Zhu, Tao, Ge: Bcl2-associated athanogene 3 interactome analysis reveals a new role in modulating proteasome activity. in Molecular & cellular proteomics : MCP 2013
findings showed that the P209L mutation causes BAG3 to aggregate; proposed that the gradual loss of available BAG3(wt) and BAG3(P209L) proteins results in insufficiency leading to myofibrillar disintegration
Data show although no any significant differences between patient groups and lean subjects of proteins SYT4 (show SYT4 Proteins), BAG3, APOA1 (show APOA1 Proteins), and VAV3 (show VAV3 Proteins), except for VGF (show VGF Proteins) protein, there was a trend between the expression of these four genes and their protein levels.
our findings suggest the existence of a so-far unrecognized quality control mechanism involving BAG3, HSPB8 (show HSPB8 Proteins) and p62/SQSTM1 (show SQSTM1 Proteins) for accurate remodelling of actin-based mitotic structures that guide spindle orientation.
BAG3 promotes pancreatic ductal adenocarcinoma growth by activating stromal macrophages.
BAG3-mediated miRNA let-7g and let-7i inhibit proliferation and enhance apoptosis of human esophageal carcinoma cells by targeting the drug transporter ABCC10 (show ABCC10 Proteins) and modulates cisplatin resistance.
This newly described ERa-mediated and estrogen response element (ERE)-independent non-canonical autophagy pathway, which involves the function of BAG3 and provides stress resistance in our model systems.
BAG3 protein loci is involved in the pathophysiology of systolic heart failure.
MiR (show MLXIP Proteins)-143 enhanced the tumor suppressive effect of shikonin partly through the regulation of BAG3 in glioblastoma stem cells.
The Hsp70 (show HSP70 Proteins)-Bag3 interaction may be a promising, new target for anticancer therapy.
BAG3 mutations should be considered even in cases with a mild phenotype or an adult onset
The stress response protein BAG3 may be prognostic for death in patients with acutely decompensated heart failure.
Bis is upregulated in astrocytes after hypoxia-ischemia; hypoxia-ischemia induces progressive cell death in the hippocampi of bis-positive mice, while hippocampal neurons are less vulnerable to hypoxia-ischemia in mice that lack Bis.
Deletion of the bis gene results in a marked increase in the production of corticosterone that is associated with thymic atrophy.
BAG3 and Hsc70 (show HSPA8 Proteins) interact with actin capping protein (show TMOD4 Proteins) CapZ (show CAPZA1 Proteins) to maintain myofibrillar integrity under mechanical stress.
Results indicate that Bis functions to mediate cellular regulation of the stem cell niche on the vascular compartment.
BAG3 alters the interaction between HSP70 (show HSP70 Proteins) and IKKgamma (show IKBKG Proteins), increasing availability of IKKgamma (show IKBKG Proteins) and protecting it from proteasome-dependent degradation; this, in turn, results in increased NF-kappaB (show NFKB1 Proteins) activity and survival
BAG3 is not required for muscle development, this co-chaperone appears to be critically important for maintenance of mature skeletal muscle.
The absence of Bis has considerable influences on postnatal growth and survival, possibly due to a nutritional impairment.
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.
BCL2-associated athanogene 3
, BAG family molecular chaperone regulator 3
, BAG family molecular chaperone regulator 3-like
, BCL2-binding athanogene 3
, bcl-2-binding protein Bis
, docking protein CAIR-1
, Bcl-2-binding protein Bis
, Bcl-2-interacting death suppressor
, bcl-2-associated athanogene 3