Hsp90 alpha Rabbit Polyclonal Antibody (R1510-29)

UNIPROT #

P07900

PROTEIN NAME

Hsp90 alpha

SYNONYMS

EL52 antibody;epididymis luminal secretory protein 52 antibody;Heat shock 86 kDa antibody;heat shock 90kD protein 1, alpha antibody;Heat shock 90kD protein 1, alpha like 4 antibody;heat shock 90kD protein, alpha-like 4 antibody;Heat shock 90kDa protein 1 alpha antibody;Heat shock protein 90kDa alpha (cytosolic) class A member 1 antibody;Heat shock protein HSP 90-alpha antibody;HS90A_HUMAN antibody;HSP 86 antibody;HSP86 antibody;Hsp89 antibody;HSP89A antibody;Hsp90 antibody;HSP90A antibody;HSP90AA1 antibody;HSP90ALPHA antibody;HSP90N antibody;HSPC1 antibody;HSPCA antibody;HSPCAL1 antibody;HSPCAL4 antibody;HSPN antibody;LAP 2 antibody;LAP2 antibody;lipopolysaccharide-associated protein 2 antibody;LPS-associated protein 2 antibody;Renal carcinoma antigen NY-REN-38 antibody

SEQUENCE SIMILARITIES

Belongs to the heat shock protein 90 family.

POST-TRANSLATIONAL MODIFICATION

ISGylated.; S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1.; Ubiquitinated via 'Lys-63'-linked polyubiquitination by HECTD1. Ubiquitination promotes translocation into the cytoplasm away from the membrane and secretory pathways.

SUBCELLULAR LOCATION

Nucleus, Cytoplasm, Melanosome, Cell membrane, Mitochondrion.

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.