HSP90 Beta Recombinant Mouse Monoclonal Antibody [2-1-G3-R] (HA601176)

UNIPROT #

P08238

PROTEIN NAME

HSP90 Beta

SYNONYMS

90 kda heat shock protein beta HSP90 beta antibody;D6S182 antibody;FLJ26984 antibody;Heat shock 84 kDa antibody;Heat shock 90kD protein 1, beta antibody;Heat shock 90kDa protein 1 beta antibody;Heat shock protein 90 alpha family class B member 1 antibody;Heat shock protein 90 kDa antibody;Heat shock protein 90kDa alpha (cytosolic) class B member 1 antibody;Heat shock protein 90kDa alpha family class B member 1 antibody;Heat shock protein beta antibody;Heat shock protein HSP 90 beta antibody;Heat shock protein HSP 90-beta antibody;HS90B_HUMAN antibody;HSP 84 antibody;HSP 90 antibody;HSP 90 b antibody;HSP 90b antibody;HSP84 antibody;HSP90 BETA antibody;hsp90ab1 antibody;HSP90B antibody;HSPC2 antibody;HSPCB antibody

SUBCELLULAR LOCATION

Cytoplasm

FUNCTION

Molecular 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 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. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression.