protein

Recombinant Human BCL2-Associated Athanogene 3

MBS143814

0.01 mg

205 USD

Recombinant Protein

Recombinant Human BCL2-Associated Athanogene 3

BCL2-Associated Athanogene 3

BAG3 Human; BCL2-Associated Athanogene 3 Human Recombinant; BIS; CAIR-1; BAG-3; BAG Family Molecular Chaperone Regulator 3; Bcl-2-associated athanogene 3; Bcl-2-binding protein Bis; Docking protein CAIR-1; BAG3; MGC104307

BAG family molecular chaperone regulator 3; BAG family molecular chaperone regulator 3; BAG family molecular chaperone regulator 3; BCL2-binding athanogene 3; bcl-2-binding protein Bis; docking protein CAIR-1; BCL2-associated athanogene 3; Bcl-2-associated athanogene 3; Bcl-2-binding protein Bis; Docking protein CAIR-1

BAG3

BAG3; BAG3; BIS; MFM6; BAG-3; CAIR-1; BIS; BAG-3

BAG3_HUMAN

E Coli

575

Greater than 90% as determined by SDS-PAGE.

The BAG3 protein contains 20mM Tris buffer pH-8, 1mM EDTA, 10% glycerol and 0.1mM PMSF. Sterile filtered colorless solution.

Store at 4 degree C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degree C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

RECOMBINANT & NATURAL PROTEINS; Recombinant Proteins; B Cell Lymphoma

Description: BAG3 Human Recombinant produced in E Coli is a single, non-glycosylated polypeptide chain containing 595 amino acids (1-575 a.a.) and having a molecular mass of 63.7 kDa. The BAG3 protein is fused to a 20 amino acid His Tag at N-terminus and purified by standard chromatogrpahy techniques. Introduction: BAG3 Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. BAG3 has anti-apoptotic activity. BAG proteins participate with Hip for their binding to Hsc70/Hsp70 ATPase domain and encourage substrate release. BAG proteins have about 45 amino acid BAG domain close to the C terminus however they differ noticeably in their N-terminal regions. BAG3 includes 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 particularly with the Hsc70 ATPase domain in vitro and in mammalian cells. They bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner. BAG3 plays a role 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. BAG3 has been shown to diminish stress-induced apoptosis.

14043024

NP_004272.2

NM_004281.3

O95817

61,595 Da

Apoptosis Modulation And Signaling Pathway 198822

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]

0.01 mg

205 USD