Antibody data
- Antibody Data
- Antigen structure
- References [5]
- Comments [0]
- Validations [0]
Submit
Validation data
Reference
Comment
Report error
- Product number
- ABIN361854 - Provider product page
- Provider
- antibodies-online
- Proper citation
- Antibodies-Online Cat#ABIN361854, RRID:AB_10790738
- Product name
- anti-AHA1, Activator of Heat Shock 90kDa Protein ATPase Homolog 1 (Yeast) (AHSA1) antibody
- Antibody type
- Polyclonal
- Description
- Protein A Purified
- Reactivity
- Human, Mouse, Rat
- Host
- Rabbit
- Vial size
- 100 μL
- Storage
- -20°C
Submitted references An interaction network predicted from public data as a discovery tool: application to the Hsp90 molecular chaperone machine.
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.
EcheverrÃa PC, Bernthaler A, Dupuis P, Mayer B, Picard D
PloS one 2011;6(10):e26044
PloS one 2011;6(10):e26044
The charged linker region is an important regulator of Hsp90 function.
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
No comments: Submit comment
No validations: Submit validation data