Product Pathways - Protein Folding
HSP90 Antibody #4874
|4874S||100 µl (10 western blots)||---||In Stock||---|
|4874||carrier free and custom formulation / quantity||email request|
Already purchased this product? Write a Review.
|W||1:1000||Human, Mouse, Rat, Monkey, D. melanogaster, Zebrafish||Endogenous||90||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IHC-P=Immunohistochemistry (Paraffin)
Species predicted to react based on 100% sequence homology: Chicken, Bovine.
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 animals with synthetic peptides corresponding to human HSP90. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from HeLa, NIH/3T3, C6 and COS cells using HSP90 Antibody.
Immunohistochemical analysis of paraffin-embedded human colon carcinoma, using HSP90 Antibody.
Immunohistochemical analysis of paraffin-embedded human lung carcinoma, showing cytoplasmic and nuclear localization, using HSP90 Antibody.
Immunohistochemical analysis of paraffin-embedded human Non-Hodgkin's lymphoma, using HSP90 Antibody.
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 extend 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).
- Jo, S.K. et al. (2006) J Am Soc Nephrol 17, 3082-92. Applications: Western Blotting.
- Izumi, N. et al. (2012) Cancer Sci 103, 50-7. Applications: Western Blotting.
- Rao, T. et al. (2014) Breast Cancer Res 16, R11. Applications: Western Blotting.
Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!
- 4877 HSP90 (C45G5) Rabbit mAb
- 4872 HSP70 Antibody
- 4875 HSP90 (E289) Antibody
- 2402 HSP27 (G31) Mouse mAb
- 2401 Phospho-HSP27 (Ser82) Antibody
- 2404 Phospho-HSP27 (Ser15) Antibody
- 2405 Phospho-HSP27 (Ser78) Antibody
- 7071 Phototope®-HRP Western Blot Detection System, Anti-rabbit IgG, HRP-linked Antibody
- 7074 Anti-rabbit IgG, HRP-linked Antibody
- 7720 Prestained Protein Marker, Broad Range (Premixed Format)
- 7727 Biotinylated Protein Ladder Detection Pack
- 7003 20X LumiGLO® Reagent and 20X Peroxide
For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.