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AGS cells overexpressing BAG4 exhibited a significant increase in the percentage of cells in the G1/G0 peak and transfection of shRNA decrese demonstrated the opposite effect.
acid-induced increase in SODD expression and decrease in cell apoptosis may depend on the activation of NOX5-S and NF-kappaB1 p50 in FLO cells
SGK1.1 regulates gene transcription upon a different set of genes some of which participate in cell survival pathways (BAG-4) and others in intracellular vesicular traffic (Brox).
SODD over-expression might be correlated with the clinical classification, curative effect, and prognosis of ALL cells.
MicroRNA-26a is strongly downregulated in melanoma and induces cell death through repression of silencer of death domains (SODD).
Altered signaling of TNFalpha-TNFR1 and SODD/BAG4 is responsible for radioresistance in human HT-R15 cells.
SODD/BAG-4 is not only a silencer of TNFR1 but also a modulator of CD95 activity, regulating the balance of both death-promoting and -depressing signals
These data confirm that silencer of death domains (SODD) and death receptor 3 (DR3) are expressed in a regulated manner during renal transplant rejection, and identify DR3 as a potential inducible mediator of tubular inflammation and injury.
BAG-4 functions as a negative regulator for apobec-1-mediated apoB mRNA editing
Gene induces transformed phenotype when overexpressed in a cancer breast cell line.
results of analysis of the genome-wide scan data was a 20 cM region at 8p11-23 in which markers had LODs > or =1.0. Linkage and association analyses of these SNPs yield suggestive results for markers in FGFR1 and BAG4.
Vincristine induces Jurkat cell apoptosis by downregulating expression of SODD protein and priming the death receptor pathway.
Silencer of death domains (SODD) inhibits skeletal muscle and kidney enriched inositol 5-phosphatase (SKIP) and regulates phosphoinositide 3-kinase (PI3K)/Akt signaling to the actin cytoskeleton.
Results suggest that silencer of death domains protein (SODD) is critical for the regulation of tumor necrosis factor signaling.
our data do not support the concept of a unique, nonredundant role of SODD for the functions of TNFR1, Hsp70, and DR3.
The proapoptotic proteins Bak (Bcl-2 antagonistic killer) and Bax (Bcl-2-associated X protein) were depleted in livers from TCPOBOP-treated CAR+/+ mice.
The protein encoded by this gene is a member of the BAG1-related protein family. BAG1 is an anti-apoptotic protein that functions through interactions with a variety of cell apoptosis and growth related proteins including BCL-2, Raf-protein kinase, steroid hormone receptors, growth factor receptors and members of the heat shock protein 70 kDa family. This protein contains a BAG domain near the C-terminus, which could bind and inhibit the chaperone activity of Hsc70/Hsp70. This protein was found to be associated with the death domain of tumor necrosis factor receptor type 1 (TNF-R1) and death receptor-3 (DR3), and thereby negatively regulates downstream cell death signaling. The regulatory role of this protein in cell death was demonstrated in epithelial cells which undergo apoptosis while integrin mediated matrix contacts are lost. Alternatively spliced transcript variants encoding distinct isoforms have been identified.
BAG family molecular chaperone regulator 4
, BAG-family molecular chaperone regulator-4
, bcl-2-associated athanogene 4
, silencer of death domains
, BCL2-associated athanogene 4