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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 Proteine (19) und BAG3 Kits (12) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 127 products:
Human Polyclonal BAG3 Primary Antibody für ICC, IF - ABIN4282959
Goldman, Chen, Roesly, Hill, Tome, Dvorak, Bernstein, Dvorak: Characterization of squamous esophageal cells resistant to bile acids at acidic pH: implication for Barrett's esophagus pathogenesis. in American journal of physiology. Gastrointestinal and liver physiology 2011
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Human Polyclonal BAG3 Primary Antibody für IHC, ELISA - ABIN1452054
Lee, Takahashi, Yasuhara, Inazawa, Kamada, Tsujimoto: Bis, a Bcl-2-binding protein that synergizes with Bcl-2 in preventing cell death. in Oncogene 2000
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Cow (Bovine) Polyclonal BAG3 Primary Antibody für WB - ABIN2783302
Franceschelli, Rosati, Lerose, De Nicola, Turco, Pascale: Bag3 gene expression is regulated by heat shock factor 1. in Journal of cellular physiology 2008
Human Polyclonal BAG3 Primary Antibody für ELISA, WB - ABIN184770
Doong, Price, Kim, Gasbarre, Probst, Liotta, Blanchette, Rizzo, Kohn: CAIR-1/BAG-3 forms an EGF-regulated ternary complex with phospholipase C-gamma and Hsp70/Hsc70. in Oncogene 2000
Human Polyclonal BAG3 Primary Antibody für IHC, IHC (p) - ABIN4282955
Nymoen, Hetland Falkenthal, Holth, Ow, Ivshina, Tropé, Kuznetsov, Staff, Davidson: Expression and clinical role of chemoresponse-associated genes in ovarian serous carcinoma. in Gynecologic oncology 2015
This study therefore identifies both BAG3 reduction and autophagy promotion as potential therapies for FLNC (zeige FLNC Antikörper)(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 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 Antikörper) 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 Antikörper)-BAG3-HSP70 (zeige HSP70 Antikörper) 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 bound to Hsp70 (zeige HSP70 Antikörper) at the same time as Hsp22 (zeige HSPB8 Antikörper), Hsp27 (zeige HSPB1 Antikörper), or alphaB-crystallin (zeige CRYAB Antikörper), suggesting that it might physically bring the chaperone families together into a complex.
These results suggest that Bag1 (zeige BAG1 Antikörper) and Bag3 control the stability of the Hsc70 (zeige HSPA8 Antikörper)-client complex using at least two distinct protein-protein contacts, providing a previously under-appreciated layer of molecular regulation in the human Hsc70 (zeige HSPA8 Antikörper) system.
we report the first mammalian model of a single amino acid mutation of BAG3 (P209L) in exon 3 of Bag3 associated with the development of muscle disease with left ventricular dysfunction and heart failure
High BAG3 expression Correlates with Sebaceous Gland Carcinoma of the Eyelid.
These results indicate a possible role for BAG3 protein in the maintenance of cell survival in endometrioid endometrial cancer.
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 Antikörper)+) channel provide novel insight into the role of BAG3 in cardiomyopathies and increased arrhythmia risks in heart failure.
molecular association of MyHC (zeige MYH13 Antikörper) and BIS is necessary for MyHC (zeige MYH13 Antikörper) 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 (zeige HSPA8 Antikörper) interact with actin capping protein (zeige TMOD4 Antikörper) CapZ (zeige CAPZA1 Antikörper) 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.
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