Recombinant Rabbit monoclonal primary
BAG2 Recombinant Rabbit Monoclonal Antibody [JE47-57] (ET7109-62)
Synthetic peptide within n-terminal human bag2.
Jurkat cell lysates, Hela cell lysate, A549 cell lysate, K562 cell lysate, HepG2 cell lysate, Hela.
Store at +4C after thawing. Aliquot store at -20C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A affinity purified.
BAG 2 antibody; BAG family molecular chaperone regulator 2 antibody; BAG-2 antibody; BAG-family molecular chaperone regulator-2 antibody; Bag2 antibody; BAG2_HUMAN antibody; BCL 2 associated athanogene 2 antibody; Bcl-2-associated athanogene 2 antibody; BCL2 associated athanogene 2 antibody; BCL2-associated athanogene 2 antibody; dJ417I1.2 (BAG family molecular chaperone regulator 2) antibody; dJ417I1.2 antibody; KIAA0576 antibody; MGC149462 antibody; OTTHUMP00000016668 antibody
Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. An increasing number of studies have indicated that BAG2 is involved in the pathogenesis of various diseases, including cancers and neurodegenerative diseases. 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.