Product: Esomeprazole (potassium salt)
TRAP1 Antibody (9B6) Summary
| Immunogen |
Recombinant human TRAP1.
|
| Isotype |
IgG2
|
| Clonality |
Monoclonal
|
| Host |
Mouse
|
| Gene |
TRAP1
|
| Purity |
Protein G purified
|
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|
Applications/Dilutions
| Dilutions |
|
| Application Notes |
This antibody is useful in Western Blot (Detects a band of ~72kDa).
|
Reactivity Notes
Human and Mouse. Please note that this antibody is reactive to Mouse and derived from the same host, Mouse. Additional Mouse on Mouse blocking steps may be required for IHC and ICC experiments. Please contact Technical Support for more information.
Packaging, Storage & Formulations
| Storage |
Store at -20C. Avoid freeze-thaw cycles.
|
| Buffer |
PBS (pH 7.2) and 50% Glycerol
|
| Preservative |
0.09% Sodium Azide
|
| Purity |
Protein G purified
|
Alternate Names for TRAP1 Antibody (9B6)
- HSP 75
- HSP75TNFR-associated protein 1
- HSP90Lheat shock protein 75 kDa, mitochondrial
- TNF receptor-associated protein 1
- TRAP-1
- tumor necrosis factor type 1 receptor associated protein
- Tumor necrosis factor type 1 receptor-associated protein
Background
The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress. It includes cytoplasmic (Hsp90-alpha/beta), ER (Grp94) and mitochondrial (TRAP1) localized members. Hsp90 is structurally composed of an N-terminal ATP binding domain, a medial substrate-binding region, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones to stabilize a multitude of client protein substrates. TRAP1 (aka Hsp75) was originally identified as a chaperone binding partner for retinoblastoma protein. TRAP1 was later found by immunofluorescence to be localized to the mitochondria. TRAP1 is significantly more active as an ATPase due in part to the lack of regulatory elements in the C-terminus, but retains the ability to dimerize. However, it does not form stable complexes with typical cochaperones of Hsp90 like p23 and HOP4. Recently TRAP1 has been identified as a protective element for cell survival, and has been suggested as a novel target for anti-cancer therapeutics.
