Hsp90 beta Recombinant Rabbit Monoclonal Antibody [SY46-01] (ET1605-56)

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

SEQUENCE SIMILARITIES

Belongs to the heat shock protein 90 family.

POST-TRANSLATIONAL MODIFICATION

Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro).; ISGylated.; S-nitrosylated; negatively regulates the ATPase activity.; Phosphorylation at Tyr-301 by SRC is induced by lipopolysaccharide. Phosphorylation at Ser-226 and Ser-255 inhibits AHR interaction.; Methylated by SMYD2; facilitates dimerization and chaperone complex formation; promotes cancer cell proliferation.; Cleaved following oxidative stress resulting in HSP90AB1 protein radicals formation; disrupts the chaperoning function and the degradation of its client proteins.

SUBCELLULAR LOCATION

Cytoplasm, Melanosome,Nucleus,Secreted,Cell membrane,Dynein axonemal particle .

FUNCTION

The heat shock response was first described for Drosophila salivary gland cells and morphologically consists of a change in their polytene chromosome puffing patterns that involves de novo synthesis of a few proteins. Similar heat shock proteins were later discovered in bacterial chicken and mammalian cells, and have been subsequently studied in other organisms. A series of proteins including HSP 90, HSP 70, HSP 20-30 and ubiquitin are induced by insults such as temperature shock, chemicals and other environmental stress. A major function of HSP 90 and other HSPs is to act as molecular chaperones. HSP 90 forms a complex with glucocorticoid receptor (GR), rendering the non ligand-bound receptor transcriptionally inactive. HSP 90 binds the GR as a heterocomplex composed of either HSP 56 or Cyclophilin D, forming an aporeceptor comiplex. HSP 90 also exists as a dimer with other proteins such as p60/sti1 and p23, forming an apo-receptor complex with estrogen and androgen receptors.