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|Product Name||BAG3, 1-575aa, Human|
|Background||BAG3 was reported initially as a protein-refolding cochaperone of the bcl2 binding protein BAG family and as upregulated in response to persistent stress of cellular calcium balance dysregulation. 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. Also, it has been shown to diminish stress-induced apoptosis. Recombinant human BAG3, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.|
|Synonyms||BIS, CAIR-1, BAG family molecular chaperone regulator 3 BAG 3, Bcl 2 binding protein, BCL2 associated athanogene 3, BCL2 binding athanogene 3, Docking protein CAIR 1.|
|AA Sequence||MGSSHHHHHH SSGLVPRGSH MSAATHSPMM QVASGNGDRD PLPPGWEIKI DPQTGWPFFV DHNSRTTTWN DPRVPSEGPK ETPSSANGPS REGSRLPPAR EGHPVYPQLR PGYIPIPVLH EGAENRQVHP FHVYPQPGMQ RFRTEAAAAA PQRSQSPLRG MPETTQPDKQ CGQVAAAAAA QPPASHGPER SQSPAASDCS SSSSSASLPS SGRSSLGSHQ LPRGYISIPV IHEQNVTRPA AQPSFHQAQK THYPAQQGEY QTHQPVYHKI QGDDWEPRPL RAASPFRSSV QGASSREGSP ARSSTPLHSP SPIRVHTVVD RPQQPMTHRE TAPVSQPENK PESKPGPVGP ELPPGHIPIQ VIRKEVDSKP VSQKPPPPSE KVEVKVPPAP VPCPPPSPGP SAVPSSPKSV ATEERAAPST APAEATPPKP GEAEAPPKHP GVLKVEAILE KVQGLEQAVD NFEGKKTDKK YLMIEEYLTK ELLALDSVDP EGRADVRQAR RDGVRKVQTI LEKLEQKAID VPGQVQVYEL QPSNLEADQP LQAIMEMGAV AADKGKKNAG NAEDPHTETQ QPEATAAATS NPSSMTDTPG NPAAP|
|Molecular Weight||27.7 kDa (248aa), confirmed by MALDI-TOF.|
|Form||Liquid, in 20mM Tris-HCl buffer (pH8.0) containing 50mM NaCl, 10% glycerol|
|Concentration||1 mg/ml (determined by Bradford assay)|
|Purity||> 90% by SDS-PAGE|
|Storage||Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -20C or -70C. Avoid repeated freezing and thawing cycles.|
|Intended Use||For Research Use Only|
|References||Virador VM., et al. (2009) PLos One. 4(4):e5136.
Kyratsous CA., et al. (2008) Proc Natl Acad Sci U S A. 105(52):20912-7.
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