Hsp75/TRAP1 Mouse, Unlabeled, Clone: 42, BD

Description

• 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