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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 Proteins (19) and BAG3 Kits (12) and many more products for this protein.
Showing 10 out of 124 products:
Human Polyclonal BAG3 Primary Antibody for 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
Show all 4 references for ABIN4282959
Human Polyclonal BAG3 Primary Antibody for 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
Show all 2 references for ABIN1452054
Cow (Bovine) Polyclonal BAG3 Primary Antibody for 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 for 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 for 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
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
BAG3 bound to Hsp70 (show HSP70 Antibodies) at the same time as Hsp22 (show HSPB8 Antibodies), Hsp27 (show HSPB1 Antibodies), or alphaB-crystallin (show CRYAB Antibodies), suggesting that it might physically bring the chaperone families together into a complex.
These results suggest that Bag1 (show BAG1 Antibodies) and Bag3 control the stability of the Hsc70 (show HSPA8 Antibodies)-client complex using at least two distinct protein-protein contacts, providing a previously under-appreciated layer of molecular regulation in the human Hsc70 (show HSPA8 Antibodies) 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.
By showing transcription factor HSF1 (show HSF1 Antibodies) activation, we demonstrated that HCA induces the expression of BAG3 through HSF1 (show HSF1 Antibodies) activation. More importantly, knockdown of BAG3 expression using siRNA largely inhibited HCA-induced apoptosis, suggesting that BAG3 is actively involved in HCA-induced cancer cell death
BAG3 was found to positively regulate Mcl-1 (show MCL1 Antibodies) levels by binding to and inhibiting USP9X (show USP9X Antibodies). Our data show that BAG3 and Mcl-1 (show MCL1 Antibodies) are key mediators of resistance to chemotherapy in ovarian cancer
These results provide further insight into the molecular mechanisms involved in the enhancement of hyperthermia sensitivity by the silencing of BAG3 in human oral squamous cell carcinoma cells.
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
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 Antibodies)+) channel provide novel insight into the role of BAG3 in cardiomyopathies and increased arrhythmia risks in heart failure.
molecular association of MyHC (show MYH13 Antibodies) and BIS is necessary for MyHC (show MYH13 Antibodies) 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 Antibodies) interact with actin capping protein (show TMOD4 Antibodies) CapZ (show CAPZA1 Antibodies) 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 Antibodies) and IKKgamma (show IKBKG Antibodies), increasing availability of IKKgamma (show IKBKG Antibodies) and protecting it from proteasome-dependent degradation; this, in turn, results in increased NF-kappaB (show NFKB1 Antibodies) 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