BAG3 recombinant protein

BAG3, 1-575aa, Human, His tag, E Coli

Cat. Num. AAA203482

• Gene Names: BAG3; BIS; MFM6; BAG-3; CAIR-1
• Applications: SDS-Page
• Purity: > 90% by SDS-PAGE
• Synonyms: BAG3; 1-575aa; Human; His tag; E Coli; BAG family molecular chaperone regulator 3; 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.; BAG3 recombinant protein

• Host: E Coli
• Purity/Purification: > 90% by SDS-PAGE
• Form/Format: Liquid. In 20mM Tris-HCl Buffer (pH 8.0) containing 1mM EDTA, 0.1mM PMSF, 10% glycerol
• Concentration: 0.5 mg/ml (determined by Bradford assay) (varies by lot)
• 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
• Sequence Length: 575

• Applicable Applications for BAG3 recombinant protein: SDS-PAGE
• Antigen Species: Human
• Tag Information: His-tag
• Preparation and Storage: Can be stored at 4 degree C short term (1-2 weeks).; For long term storage, aliquot and store at -20 degree C or -70 degree C.; Avoid repeated freezing and thawing cycles.

SDS-Page

Related Product Information for BAG3 recombinant protein

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.

Product Categories/Family for BAG3 recombinant protein

Heat Shock Proteins

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.;

NCBI and Uniprot Product Information

• NCBI GI #: 14043024
• NCBI GeneID: 9531
• NCBI Accession #: NP_004272
• NCBI GenBank Nucleotide #: NM_004281.3
• UniProt Accession #: O95817; Q3B763; Q9NT20; Q9P120; A8K5L8
• Molecular Weight: 63.7 kDa (595aa)
• NCBI Official Full Name: BAG family molecular chaperone regulator 3
• NCBI Official Synonym Full Names: BCL2 associated athanogene 3
• NCBI Official Symbol: BAG3
• NCBI Official Synonym Symbols: BIS; MFM6; BAG-3; CAIR-1
• NCBI Protein Information: BAG family molecular chaperone regulator 3
• UniProt Protein Name: BAG family molecular chaperone regulator 3
• Protein Family: BAG family molecular chaperone regulator
• UniProt Gene Name: BAG3
• UniProt Synonym Gene Names: BIS; BAG-3

NCBI Description

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 protein encoded by this gene contains a WW domain in the N-terminal region and a BAG domain in the C-terminal region. 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. [provided by RefSeq, Jul 2008]

Uniprot Description

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).