BCL2 associated athanogene 4 ELISA Kits

BAG family proteins are highly conserved throughout eukaryotes and regulate Hsc/Hsp70-mediated molecular chaperone activities and apoptosis. BAG_1 (Bcl_2 associated athanogene_1) is a multifunctional protein, linking cell proliferation, cell death, protein folding, and cell stress. In vivo, BAG_1 is expressed in growth plate and articular cartilage, and the expression of BAG_1 is decreased with aging. A study demonstrated that BAG_1 is involved in endoplasmic reticulum (ER) stress_induced apoptosis in chondrocytes. Induction of ER stress through multiple mechanisms all resulted in downregulation of BAG_1 expression. Moreover, under ER stress conditions, the reduced expression of collagen type II was delayed in chondrocytes overexpressing BAG_1. The results suggest a novel role for BAG_1 in supporting viability and matrix expression of chondrocytes. Also, the results of two-dimensional immunoblots suggested that the phosphorylation of BAG2 was specifically controlled in a p38 MAPK-dependent manner. Thus, p38 MAPK-MAPKAP kinase 2-BAG2 phosphorylation cascade may be a novel signaling pathway for response to extracellular stresses.

BAG5 overexpression in 22Rv.1 prostate cancer cells inhibited ER-stress induced apoptosis in the unfolded protein response by suppressing PERK-eIF2-ATF4 activity while enhancing the IRE1-Xbp1 axis of this pathway. Furthermore, GRP78/BiP has been identified as a novel interaction partner of Bag5. Also, BAG6 is an essential protein that functions in two distinct biological pathways, ubiquitin-mediated protein degradation of defective polypeptides and tail-anchored (TA) transmembrane protein biogenesis in mammals. The observations of a study indicate that the BAGS domain of BAG6 promotes the TA protein biogenesis pathway in mammals by the interaction with Ubl4a.