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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 (142) and BAG3 Proteins (12) and many more products for this protein.
Showing 6 out of 18 products:
Human BAG3 ELISA Kit for Sandwich ELISA - ABIN418041
Pacheco, Berra, Morais, Sciani, Branco, Bosch, Chudzinski-Tavassi: Dynein function and protein clearance changes in tumor cells induced by a Kunitz-type molecule, Amblyomin-X. in PLoS ONE 2014
This study therefore identifies both BAG3 reduction and autophagy promotion as potential therapies for FLNC (show FLNC ELISA Kits)(W2710X) myofibrillar myopathy, and identifies protein insufficiency due to sequestration, compounded by impaired autophagy, as the cause.
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
The Hsp70 (show HSP70 ELISA Kits)-Bag3 complex therefore functions as an important signaling node that senses proteotoxicity and triggers multiple pathways that control cell physiology, including activation of protein aggregation.
study revealed oncogenic roles of BAG3 in chondrosarcoma and provided mechanisms that the BAG3-modulated the expression of RUNX2 (show RUNX2 ELISA Kits) through upregulation of beta-catenin (show CTNNB1 ELISA Kits).
BAG3 interacted with CXCR4 (show CXCR4 ELISA Kits) mRNA and promoted its expression via its coding and 3'-untranslational regions.
HSPB2 (show HSPB2 ELISA Kits) competes with HSPB8 (show HSPB8 ELISA Kits) for binding to BAG3. In contrast, HSPB3 (show HSPB3 ELISA Kits) negatively regulates HSPB2 (show HSPB2 ELISA Kits) association with BAG3.
Silencing of HSPB8 markedly decreased the mitotic levels of BAG3 in HeLa cells, supporting its crucial role in BAG3 mitotic functions. The results support a role for the HSPB8-BAG3 chaperone complex in quality control of actin-based structure dynamics that are put under high tension, notably during cell cytokinesis.
Our findings suggest that high levels of BIS expression might confer stem-cell-like properties on cancer cells through STAT3 (show STAT3 ELISA Kits) stabilization
modulation of proteostasis is a distinct biological function of sAPPalpha and does not require surface-bound holo-APP (show APP ELISA Kits).
higher levels of BAG3 were observed in hypertensive patients compared to healthy controls, and even higher levels in hypertensive diabetic patients compared to healthy subjects.
BAG3 directly stabilizes hexokinase 2 (show HK2 ELISA Kits) mRNA and promotes aerobic glycolysis in pancreatic cancer cells.
These results indicated that at least some oncogenic functions of BAG3 were mediated through posttranscriptional regulation of Skp2 via antagonizing suppressive action of miR (show MLXIP ELISA Kits)-21-5p in ovarian cancer cells.
Thus, BAG3 is critical for the protein turnover of small HSPs via activation of autophagy in the heart.
BAG3 plays a relevant role in regulating SNCA clearance via macroautophagy, and the heat shock protein 70 (show HSP70 ELISA Kits)-BAG3-sequestosome 1 (show SQSTM1 ELISA Kits) complex may be involved in this process.
BAG3 expression is required for neuronal differentiation and migration.
interaction between BAG3 and HSP70 (show HSP70 ELISA Kits) is essential for BAG3 to stabilize small heat shock proteins and maintain cardiomyocyte protein homeostasis
The spatial regulation of mTORC1 exerted by BAG3 apparently provides the basis for a simultaneous induction of autophagy and protein synthesis to maintain the proteome under mechanical strain.
Genetic variation in BAG3 plays an important role in the prevention of ischemic tissue necrosis.
The aim of this study was to investigate the possible hemodynamic effects of BAG3 performing both in vitro and in vivo experiments.
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 ELISA Kits)+) 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.
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