Cell Signaling Technology

Product Pathways - Protein Folding/Stability

HSP90 Antibody #4874

Applications Reactivity Sensitivity MW (kDa) Source
W IHC-P H M R Mk Dm (C) (B) (Z) Endogenous 92 Rabbit

Applications Key:  W=Western Blotting  IHC-P=Immunohistochemistry (Paraffin)
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  C=Chicken  B=Bovine  Dm=D. melanogaster  Z=Zebra Fish
Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

HSP90 Antibody detects endogenous levels of total HSP90 protein, alpha and beta isoforms. This antibody does not cross-react with other HSPs.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with synthetic peptides (KLH-coupled) corresponding to human HSP90. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa, NIH/3T3, C6 and COS cells using HSP90 Antibody.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human colon carcinoma, using HSP90 Antibody.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human lung carcinoma, showing cytoplasmic and nuclear localization, using HSP90 Antibody.


IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human Non-Hodgkin's lymphoma, using HSP90 Antibody.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human prostate carcinoma, using HSP90 Antibody.

Background

HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP and co-chaperone dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 go beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).

  1. Nollen, E.A. and Morimoto, R.I. (2002) J. Cell Sci. 115, 2809-2816.
  2. Young, J.C. et al. (2003) Trends Biochem. Sci. 28, 541-547.
  3. Pratt, W.B. and Toft, D.O. (2003) Exp. Biol. Med. 228, 111-133.
  4. Hohfeld, J. et al. (2001) EMBO Rep. 2, 885-890.

Application References

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Companion Products

This product is for in vitro research use only and is not intended for use in humans or animals. This product is not intended for use as therapeutic or in diagnostic procedures.

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