|Application ||WB, E|
|Other Accession||NP_004273, 9532|
|Calculated MW||23772 Da|
|Other Names||BAG family molecular chaperone regulator 2, BAG-2, Bcl-2-associated athanogene 2, BAG2|
|Format||0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin|
|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||Goat Anti-BAG2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release.|
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Provided below are standard protocols that you may find useful for product applications.
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.
Large-scale mapping of human protein-protein interactions by mass spectrometry. Ewing RM, et al. Mol Syst Biol, 2007. PMID 17353931.
The LIFEdb database in 2006. Mehrle A, et al. Nucleic Acids Res, 2006 Jan 1. PMID 16381901.
Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. Kimura K, et al. Genome Res, 2006 Jan. PMID 16344560.
BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. Arndt V, et al. Mol Biol Cell, 2005 Dec. PMID 16207813.
Regulation of the cytoplasmic quality control protein degradation pathway by BAG2. Dai Q, et al. J Biol Chem, 2005 Nov 18. PMID 16169850.
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