Bag6 (BCL2 associated athanogene 6) is a multifunctional chaperone involved in tail anchored protein biogenesis, endoplasmic reticulum-associated protein degradation, and degradation of mislocalized membrane proteins. It is the central component of a stable three chaperone complex that also contains two cofactors-Ubl4A and Trc35. This complex acts in conjunction with the co-chaperone SGTA to channel proteins bearing an exposed hydrophobic segment in the cytosol to avoid protein aggregation. The complex also associates with several ubiquitin ligases including gp78 and RNF126, which link it to protein quality control of misfolded or mislocalized polypeptides. This is one of the antibodies used to confirm the that all three proteins were associated with gp78.
- This is a research tool that may be used to study protein quality control in mammalian cells
- May be of use in creating novel anti-retroviral treatments
- A novel, robust mechanism to model mammalian cell protein integrity