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BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. Zusätzlich bieten wir Ihnen BAG3 Antikörper (130) und BAG3 Proteine (11) und viele weitere Produktgruppen zu diesem Protein an.
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Human BAG3 ELISA Kit für 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 (zeige 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
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 (zeige 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 (zeige MLXIP ELISA Kits)-21-5p in ovarian cancer cells.
Familial suffering of Dilated cardiomyopathy and carrying a heterozygous large deletion in the BAG3 gene.This gene encodes BCL2-associated athanogene 3 protein.
BAG3 mutations are associated with DCM phenotypes. BAG3 should be added to cardiomyopathy gene panels for screening of DCM patients, and patients previously considered gene elusive should undergo sequencing of the BAG3 gene.
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.
variants in TNNT2 (zeige TNNT2 ELISA Kits) and BAG3 are associated with a high propensity to life-threatening cardiomyopathy presenting from childhood and young adulthood.
It has been demonstrated that HSPB8 (zeige HSPB8 ELISA Kits)-BAG3-HSP70 (zeige HSP70 ELISA Kits) ensures the functionality of stress granules and restores proteostasis by targeting defective ribosomal products for degradation.
The authors propose that the chaperone-mediated autophagy function of BAG3 represents a specific host defense strategy to counteract the function of VP40 in promoting efficient egress and spread of virus particles.
BAG3 plays a relevant role in regulating SNCA clearance via macroautophagy, and the heat shock protein 70 (zeige HSP70 ELISA Kits)-BAG3-sequestosome 1 (zeige SQSTM1 ELISA Kits) complex may be involved in this process.
BAG3 expression is required for neuronal differentiation and migration.
interaction between BAG3 and HSP70 (zeige HSP70 ELISA Kits) is essential for BAG3 to stabilize small heat shock proteins and maintain cardiomyocyte protein homeostasis
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 (zeige 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.
BAG3 promotes pancreatic ductal adenocarcinoma growth by activating stromal macrophages.
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