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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 (121) and BAG3 Proteins (14) and many more products for this protein.
Showing 7 out of 12 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
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 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 ELISA Kits), BAG3, APOA1 (show APOA1 ELISA Kits), and VAV3 (show VAV3 ELISA Kits), except for VGF (show VGF ELISA Kits) 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 ELISA Kits) and p62/SQSTM1 (show SQSTM1 ELISA Kits) 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 ELISA Kits) 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 ELISA Kits)-143 enhanced the tumor suppressive effect of shikonin partly through the regulation of BAG3 in glioblastoma stem cells.
The Hsp70 (show HSP70 ELISA Kits)-Bag3 interaction may be a promising, new target for anticancer therapy.
molecular association of MyHC and BIS is necessary for MyHC stabilization in skeletal muscle.
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 ELISA Kits) interact with actin capping protein (show TMOD4 ELISA Kits) CapZ (show CAPZA1 ELISA Kits) 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 ELISA Kits) and IKKgamma (show IKBKG ELISA Kits), increasing availability of IKKgamma (show IKBKG ELISA Kits) and protecting it from proteasome-dependent degradation; this, in turn, results in increased NF-kappaB (show NFKB1 ELISA Kits) 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