Heat shock protein 90 alpha family class B member 1
Heat shock protein 90 kDa
Heat shock protein 90kDa alpha (cytosolic) class B member 1
Heat shock protein 90kDa alpha family class B member 1
Heat shock protein beta
Heat shock protein HSP 90 beta
Heat shock protein HSP 90-beta
HSP 90 b
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.
Post-translational modificationsUbiquitinated in the presence of STUB1-UBE2D1 complex (in vitro). ISGylated. S-nitrosylated; negatively regulates the ATPase activity.
Cellular localizationCytoplasm. Melanosome. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Lane 1: ab80353 on 10% SDS-PAGE, Coomassie staining, 3µg. Lane 2: Protein marker.
References for Recombinant Human Hsp90 beta protein (ab80353)
This product has been referenced in:
Christensen B et al. Erythropoietin does not activate erythropoietin receptor signaling or lipolytic pathways in human subcutaneous white adipose tissue in vivo. Lipids Health Dis15:160 (2016).
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