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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 (122) and BAG3 Kits (9) 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
high expression of BAG3 was detected in a majority of medulloblastoma tissues and predicted poor outcome for medulloblastoma patients.
in the present study, we demonstrated that BAG3 overexpression plays a critical role in cell proliferation, migration, and invasion of colorectal cancer. Our data suggests targeted inhibition of BAG3 may be useful for patients with colorectal cancer
BAG3 maintains the basal amount of LC3B (show MAP1LC3B Proteins) protein by controlling the translation of its mRNA in HeLa and HEK293 cells.
Data indicate a tumor suppressor-like function of Bcl-2 associated athanogene 3 (BAG3) via direct interaction with glucose 6 phosphate dehydrogenase (G6PD (show G6PD Proteins)) in hepatocellular carcinomas (HCCs (show HCCS Proteins)) at the cellular level.
BAG3 is associated with Z-disc maintenance.
BAG3 is a suitable target for combined therapies aimed at synergistically inducing apoptosis in bladder cancer.
The present study, for the first time, examined the expression of central autophagy proteins BAG3 and p62 in testicular cancer
Bis expression was higher in squamous cell carcinoma than in adenocarcinoma in Lung Cancer.
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.
Our findings that BAG3 is localized at the sarcolemma and t-tubules while modulating myocyte contraction and action potential duration through specific interaction with the beta1-adrenergic receptor and L-type Ca(2 (show CA2 Proteins)+) channel provide novel insight into the role of BAG3 in cardiomyopathies and increased arrhythmia risks in heart failure.
molecular association of MyHC and BIS is necessary for MyHC stabilization in skeletal muscle.
BAG3 promotes pancreatic ductal adenocarcinoma growth by activating stromal macrophages.
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