|Calculated MW||61595 Da|
|Other Names||BAG family molecular chaperone regulator 3, BAG-3, Bcl-2-associated athanogene 3, Bcl-2-binding protein Bis, Docking protein CAIR-1, BAG3, BIS|
|Target/Specificity||A synthetic peptide corresponding to residues in human Bag-3 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||YWHAE Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70 (PubMed:9873016, PubMed:27474739). Has anti-apoptotic activity (PubMed:10597216). Plays a role in the HSF1 nucleocytoplasmic transport (PubMed:26159920).|
|Cellular Location||Nucleus. Cytoplasm. Note=Colocalizes with HSF1 to the nucleus upon heat stress (PubMed:26159920)|
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Provided below are standard protocols that you may find useful for product applications.
Bcl-2-associated athanogene 3 (Bag-3) is a member of a conserved family of cyto-protective proteins that bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone acitivity in a Hip-repressible manner. It has been shown to be prominently expressed in striated muscle and colocalizes with Z-disks. Bag-3 is not required for muscle development, but appears to be critically important for maintenance of mature skeletal muscle (1-2). Bag-3 has also been shown to have anti-apoptotic activity (3). Overexpression of Bag-3 has prevented or reduced the distraction of polyubiquitinated Hsp90/Hsp70 client proteins such as Cyclin D1, Akt, glycogen synthase 3B, and p70s6 kinase, and facilitated cell survival (4).
1. Homma S, et al. Am J Pathol. 169(3):761-73, 2006 2. NCBI Reference Sequence (RefSeq): a curated non- redundant sequence database of genomes, transcripts and proteins Pruitt KD, Tatusova, T, Maglott DR Nucleic Acids Res 2007 Jan 1;35(Database issue):D61-5 3. The UniProt Consortium. The Universal Protein Resource (UniProt). Nucleic Acids Res. 36:D190-D195 (2008) 4. Virador VM., et al. PLoS One 4(4):e5136, 2009
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