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The protein encoded by BAG5 is a member of the BAG1-related protein family. Additionally we are shipping BAG5 Antibodies (163) and many more products for this protein.
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BAG5 was found as a expression variability marker in an 8-cell human embryo.
Subsequent BAG5 upregulation ameliorated the tumor-suppressive effects of miR (show MLXIP Proteins)-127-3p overexpression in epithelial ovarian cancer (EOC). In conclusion, miR (show MLXIP Proteins)-127-3p functions as a tumor suppressor in EOC, and its influence on EOC is directly through regulation of BAG5.
High BAG5 expression is associated with pancreatic cancer.
This study showed that BAG2 (show BAG2 Proteins) (Bcl-2 (show BCL2 Proteins) associated athanogene family protein 2) and BAG5 (Bcl-2 (show BCL2 Proteins)-associated athanogene family protein 5 (show CAPS Proteins)) stabilise pathogenic ataxin3-80Q by inhibiting its ubiquitination.
BAG5 protects against mitochondrial oxidative damage through regulating PINK1 (show PINK1 Proteins) degradation.
BAG5 is a binding partners of LRRK2 and part of a complex that promotes clearance of Golgi-derived vesicles through the autophagy-lysosome system.
Bag5 is overexpressed in prostate cancer and plays a role in endoplamic reticulum-stress induced apoptosis. Furthermore we have identified GRP78/BiP (show HSPA5 Proteins) as a novel interaction partner of Bag5.
BAG5 directly interacts with Parkin and stabilizes Parkin via the ubiquitin-mediated proteasomal pathway.
A novel function for BAG5 as a modulator of CHIP E3 ubiquitin ligase (show MUL1 Proteins) activity with implications for CHIP-mediated regulation of alpha-syn oligomerization.
We replicated the association of BCL2L11 (show BCL2L11 Proteins) and CASP9 (show CASP9 Proteins) with non-Hodgkin's lymphoma risk at the gene and SNP level, and identified novel associations with BCLAF1 and BAG5.
knockdown of Bag5 exacerbated Abeta1-42-induced apoptosis.
Bcl-2-associated athanogene 5 (BAG5) is a negative regulator of both Hsp70 and parkin function that sensitizes dopaminergic neurons to injury-induced death.
Here, the authors determined crystal structures of AtBAG5 alone and in complex with Ca(2+)-free CaM. Structural and biochemical studies revealed that Ca(2+)-free CaM and Hsc70 bind AtBAG5 independently, whereas Ca(2+)-saturated CaM and Hsc70 bind AtBAG5 with negative cooperativity.
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. Three transcript variants encoding two different isoforms have been found for this gene.
BAG family molecular chaperone regulator 5
, BAG-family molecular chaperone regulator-5
, bcl-2-associated athanogene 5
, BCL2-associated athanogene 5
, BAG-family molecular chaperone regulator-5 (BAG-5)
, BAG family molecular chaperone regulator 5-like