BAG2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 231 amino acids (1-211 a.a.) and having a molecular mass of 25.9kDa. The BAG2 is purified by proprietary chromatographic techniques.
BCL2-associated athanogene 2 (BAG2) belongs to the Bag family of proteins. BAG2 is a chief component of the HSC 70/CHIP chaperone-dependent ubiquitin ligase complex and acts to upset CHIP-mediated ubiquitylation. BAG proteins compete with Hip for attaching to the Hsc70/Hsp70 ATPase domain and promote substrate discharge. All the BAG proteins have a roµghly 45 amino acid BAG domain by the C-terminus but vary clearly in their N-terminal regions. The BAG domains of BAG1, BAG2, and BAG3 act together expressly with the Hsc70 ATPase domain in vitro and in mammalian cells. All three proteins attach with high affinity to the ATPase domain of Hsc70 and obstruct its chaperone activity in a Hip-repressible manner.
BAG family molecular chaperone regulator 2, BAG-2, Bcl-2-associated athanogene 2, BAG2, KIAA0576, MGC149462, dJ417I1.2.
Sterile Filtered colorless solution.
The BAG2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 0.1M NaCl.
BAG2 should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.