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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 BAG2 Antibodies (99) and many more products for this protein.
Showing 9 out of 11 products:
the nucleotide exchange factor (NEF) Bag2 stimulates SV40 release from Hsc70, thereby enabling successful virus arrival at the cytosol, which leads to infection. Hsp105, another NEF of Hsc70, displays a function overlapping that of Bag2, underscoring the importance of this release reaction.
A comprehensive review of the structure, functions, and protein interactions of BAG2
Data show that BAG2 Inhibits CHIP-Mediated HSP72 ubiquitination in aged cells.
repression of BAG2 expression or BAG2 activity by cold-sensitive pathways, as modeled in undifferentiated and differentiated cells, respectively, may be a causal factor in the accumulation of cytotoxic hyperphosphorylated tau protein.
NF-kappaB-mediated modulation of BAG2 expression regulates the shift between the neurotrophic and neurotoxic effects of Abeta1-42.
Thus, BAG2 promotes mutant p53 accumulation and gain-of-function in tumor growth, metastasis and chemoresistance.
This study showed that BAG2 (Bcl-2 associated athanogene family protein 2) and BAG5 (Bcl-2-associated athanogene family protein 5) stabilise pathogenic ataxin3-80Q by inhibiting its ubiquitination
we measured the binding of human Hsp72 (HSPA1A) to BAG1, BAG2, BAG3, and the unrelated NEF Hsp105. These studies revealed a clear hierarchy of affinities: BAG3 > BAG1 > Hsp105 >> BAG2.
this data correlate BAG2 to PINK1 for the first time, strengthening the important role of BAG2 in Parkinson disease -related neurodegeneration.
BAG2 was directly phosphorylated at serine 20 in vitro by MAPKAPK2 and MAPKAP2 is also required for phosphorylation of BAG2 in vivo.
BAG2 binds to the carboxyl terminus of Hsp70-interacting protein (CHIP) and provides a cochaperone-dependent regulatory mechanism for preventing unregulated ubiquitylation of misfolded proteins by CHIP
The activity of BAG-2 resembles that of the previously characterized Hsc70 cochaperone and CHIP inhibitor HspBP1.
findings support the notion that BAG2 is an upstream regulator of the PINK1/PARKIN signaling pathway.
Native Bag2-NTD crystals diffracted to 2.27 A resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 75.5, b = 84.7, c = 114.1 A
Free and Hsc70-bound crystal structures of Bag2-BNB show its dimeric structure, in which a flanking linker helix and loop bind to Hsc70 to promote nucleotide exchange.
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 predicted BAG2 protein contains 211 amino acids. 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 2
, BAG family molecular chaperone regulator 2
, putative BCL2-associated athanogene 2
, BAG-family molecular chaperone regulator-2
, bcl-2-associated athanogene 2
, dJ417I1.2 (BAG-family molecular chaperone regulator 2)