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.

Format

Suggested Companion Products

Preparation and Storage

The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.Store undiluted at -20°C.

Product Notices

1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to www.bdbiosciences.com/pharmingen/protocols for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.