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.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIP
recommended for detection of Ser 254 phosphorylated HSP 90 of human and mouse origin and correspondingly phosphorylated Ser 255 of rat origin by WB and IP
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to phosphorylated Ser 254 of HSP 90 of human origin
Tissue Specificity
epitope corresponding to phosphorylated Ser 254 of HSP 90 of human origin
Blots were probed with p-HSP 90 (Ser 254): preincubated with its cognate phosphorylated peptide (A) and p-HSP 90 (Ser 254): (B).
Application Notes
recommended for detection of Ser 254 phosphorylated HSP 90 of human and mouse origin and correspondingly phosphorylated Ser 255 of rat origin by WB and IP
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.