Hsp75/Trap1 Mouse, Unlabeled, Clone: 42, Bd, Mouse Monoclonal Antibody, Each

Details:

The hsp90 family of molecular chaperones is involved in a number of signal transduction pathways, including cell division, protein folding and transport. A new member of this family was recently identified as trap1 (tumor necrosis factor receptor-associated protein) or hsp75. Trap1 is a mitochondrial protein that is an atpase and atp-binding protein, rendering it similar to hsp90. There is a high degree of homology between trap1 and hsp90 in 6 domains, however one major difference is that a highly charged domain present in hsp90 is absent in trap1. Trap1 has been shown to interact with the intracellular domain of the type 1 receptor for tumor necrosis factor (tnfr-1ic) and to the retinoblastoma protein (rb). Signaling through tnfr-1 induces antiviral responses, fibroblast proliferation, cytotoxicity, etc. Trap1 binds tnfr-1ic outside of the death domain leading to disruption in the signaling by tnfr-1. Rb has been shown to play a pivotal role in cellular differentiation and progression through the cell cycle. Trap1 associates with rb via an lxcxe motif, which is common among proteins that interact with rb through sv40 t-antigen binding domain. Thus, trap1 is a new member of the hsp90 family that interacts with rb and tnfr-1ic.Immunofluorescence, western blotting