Antibody data
- Antibody Data
- Antigen structure
- References [4]
- Comments [0]
- Validations
- Western blot [1]
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- Product number
- ABIN2484466 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-AHA1, Activator of Heat Shock 90kDa Protein ATPase Homolog 1 (Yeast) (AHSA1) antibody (Atto 565)
- Antibody type
- Polyclonal
- Description
- Protein A Purified
- Reactivity
- Human, Mouse, Rat
- Host
- Rabbit
- Vial size
- 100 μL
- Storage
- -20°C
Submitted references The charged linker region is an important regulator of Hsp90 function.
A novel HSP90 chaperone complex regulates intracellular vesicle transport.
Silencing of HSP90 cochaperone AHA1 expression decreases client protein activation and increases cellular sensitivity to the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin.
Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation.
Hainzl O, Lapina MC, Buchner J, Richter K
The Journal of biological chemistry 2009 Aug 21;284(34):22559-67
The Journal of biological chemistry 2009 Aug 21;284(34):22559-67
A novel HSP90 chaperone complex regulates intracellular vesicle transport.
Lotz GP, Brychzy A, Heinz S, Obermann WM
Journal of cell science 2008 Mar 1;121(Pt 5):717-23
Journal of cell science 2008 Mar 1;121(Pt 5):717-23
Silencing of HSP90 cochaperone AHA1 expression decreases client protein activation and increases cellular sensitivity to the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin.
Holmes JL, Sharp SY, Hobbs S, Workman P
Cancer research 2008 Feb 15;68(4):1188-97
Cancer research 2008 Feb 15;68(4):1188-97
Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation.
Harst A, Lin H, Obermann WM
The Biochemical journal 2005 May 1;387(Pt 3):789-96
The Biochemical journal 2005 May 1;387(Pt 3):789-96
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- WB