The BAG6 antibody targets the BAG family molecular chaperone regulator 6 (BAG6), also known as BAT3 or Scythe. BAG6 is a multifunctional protein involved in protein quality control, apoptosis, and cellular stress responses. It plays a critical role in the ubiquitin-proteasome system by facilitating the degradation of mislocalized or misfolded proteins. BAG6 associates with newly synthesized membrane proteins to prevent aggregation and directs aberrant polypeptides to proteasomal or lysosomal degradation pathways. Additionally, it interacts with HSP70 and E3 ubiquitin ligases, linking chaperone activity to ubiquitination processes.
BAG6 is implicated in diverse cellular processes, including DNA damage repair, immune response modulation, and endoplasmic reticulum (ER) stress management. Its involvement in apoptosis stems from interactions with pro-apoptotic factors, such as AIF, and regulation of caspase activity. Dysregulation of BAG6 has been linked to cancers, neurodegenerative disorders, and autoimmune diseases.
The BAG6 antibody is widely used in research to study protein homeostasis, stress signaling, and disease mechanisms. Applications include Western blotting, immunoprecipitation, and immunofluorescence to assess BAG6 expression, localization, and interaction partners. Its utility extends to exploring therapeutic strategies targeting protein quality control pathways. Researchers also leverage BAG6 antibodies to investigate its role in tumor progression, neurodegeneration, and immune regulation, making it a vital tool in molecular and cellular biology.