Product Pathways - Protein Folding
HSP90 (C45G5) Rabbit mAb #4877
|4877S||100 µl (10 western blots)||---||In Stock||---|
|4877P||40 µl (4 western blots)||---||In Stock||---|
|4877||carrier free and custom formulation / quantity||email request|
Already purchased this product? Write a Review.
|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||90||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IHC-P=Immunohistochemistry (Paraffin), IF-IC=Immunofluorescence (Immunocytochemistry), F=Flow Cytometry
Species predicted to react based on 100% sequence homology: Bovine.
Specificity / Sensitivity
HSP90 (C45G5) Rabbit mAb detects endogenous levels of total HSP90 protein. This antibody does not cross-react with other HSPs.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide surrounding Asn300 of human HSP90.
Western blot analysis of extracts from HeLa, NIH/3T3, PC12 and COS cells using HSP90 (C45G5) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded human colon using HSP90 (C45G5) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded human colon carcinoma using HSP90 (C45G5) Rabbit mAb.
Flow cytometric analysis of HeLa cells using HSP90 (C45G5) Rabbit mAb (blue) compared to a nonspecific negative control antibody (red).
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).
- Thedieck, K. et al. (2013) Cell 154, 859-874. 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!
- 4875 HSP90 (E289) Antibody
- 4874 HSP90 Antibody
- 4872 HSP70 Antibody
- 4873 HSP70 (6B3) Rat mAb
- 4871 HSP40 (C64B4) Rabbit mAb
- 4876 HSP70 (D69) 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
- 8112 SignalStain® Antibody Diluent
For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.
This antibody is developed, validated, and produced by CST using in part technology under license (granting certain rights including those under U.S. Patent No. 5,675,063) from Epitomics, Inc.