BAG2 Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | O95816 |
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Clone Names | 100507034 |
Gene ID | 9532 |
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Other Names | BAG family molecular chaperone regulator 2, BAG-2, Bcl-2-associated athanogene 2, BAG2 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP14053b was selected from the C-term region of BAG2. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | BAG2 |
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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 (PubMed:24318877, PubMed:9873016). |
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Provided below are standard protocols that you may find useful for product applications.
Background
BAG proteins compete with Hip for binding to theHsc70/Hsp70 ATPase domain and promote substrate release. All theBAG proteins have an approximately 45-amino acid BAG domain nearthe C terminus but differ markedly in their N-terminal regions. Thepredicted BAG2 protein contains 211 amino acids. The BAG domains ofBAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPasedomain in vitro and in mammalian cells. All 3 proteins bind withhigh affinity to the ATPase domain of Hsc70 and inhibit itschaperone activity in a Hip-repressible manner. [provided byRefSeq].
References
Arndt, V., et al. Mol. Biol. Cell 16(12):5891-5900(2005)Dai, Q., et al. J. Biol. Chem. 280(46):38673-38681(2005)Ueda, K., et al. J. Biol. Chem. 279(40):41815-41821(2004)Ueda, K., et al. J. Biol. Chem. 279(40):41815-41821(2004)Simpson, J.C., et al. EMBO Rep. 1(3):287-292(2000)
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