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.
MGSSHHHHHH SSGLVPRGSH MAQAKINAKA NEGRFCRSSS MADRSSRLLE SLDQLELRVE ALREAATAVE QEKEILLEMI HSIQNSQDMR QISDGEREEL NLTANRLMGR TLTVEVSVET IRNPQQQESL KHATRIIDEV VNKFLDDLGN AKSHLMSLYS ACSSEVPHGP VDQKFQSIVI GCALEDQKKI KRRLETLLRN IENSDKAIKL LEHSKGAGSK TLQQNAESRF N.
The BAG family was first identified as a group of proteins that prevent cell death through their interaction with Bcl-2 . BAG2, in particular, shares a similar molecular structure and function with other BAG family members. It interacts with the ATPase domain of the heat shock protein 70 (Hsp70) through its BAG domain . This interaction is crucial for regulating various cellular functions.
BAG2 is a chief component of the HSC 70/CHIP chaperone-dependent ubiquitin ligase complex. It acts to disrupt CHIP-mediated ubiquitylation, thereby promoting substrate discharge . BAG proteins, including BAG2, compete with Hip for attaching to the Hsc70/Hsp70 ATPase domain, which is essential for their function as co-chaperones .
An increasing number of studies have indicated that BAG2 is involved in the pathogenesis of various diseases, including cancers and neurodegenerative diseases . For instance, BAG2 has been found in various types of tumor cells, including renal cell carcinoma, glioblastoma, and thyroid carcinoma cells . Its role in disease pathogenesis makes it a potential target for therapeutic approaches.