Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
FunctionMolecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.
Sequence similaritiesBelongs to the heat shock protein 90 family.
DomainThe TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1.
Post-translational modificationsISGylated. S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1.
Cellular localizationCytoplasm. Melanosome. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
ICC/IF image of ab90555 stained HeLa cells. The cells were 100% Methanol fixed (5 min) and then incubated in 1%BSA / 10% normal Goat serum / 0.3M glycine in 0.1% PBS-Tween for 1h to permeabilise the cells and block non-specific protein-protein interactions. The cells were then incubated with the antibody (ab90555, 5µg/ml) overnight at +4°C. The secondary antibody (green) was ab96899, DyLight® 488 Goat anti-Rabbit IgG (H+L) used at a 1/250 dilution for 1h. Alexa Fluor® 594 WGA was used to label plasma membranes (red) at a 1/200 dilution for 1h. DAPI was used to stain the cell nuclei (blue) at a concentration of 1.43µM.
Western blot - Hsp90 antibody (ab90555)
All lanes : Anti-Hsp90 antibody (ab90555) at 1/1000 dilution
Lane 1 : Molecular weight marker Lane 2 : HeLa Cell Lysate (Heat Shocked) Lane 3 : 3T3 Cell Lysate (Heat Shocked) Lane 4 : Rat 2 Cell Lysate (Heat Shocked)
Predicted band size : 83 kDa
References for Anti-Hsp90 antibody (ab90555)
This product has been referenced in:
Goldlust IS et al. Mouse model implicates GNB3 duplication in a childhood obesity syndrome. Proc Natl Acad Sci U S A110:14990-4 (2013).
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