Product Pathways - Protein Folding
HSP27 Antibody (Rodent Preferred) #2442
PhosphoSitePlus® protein, site, and accession data: HSP27
| Applications | Reactivity | Sensitivity | MW (kDa) | Source |
|---|---|---|---|---|
| W IF-IC F | M R | Endogenous | 27 | Rabbit |
Applications Key:
W=Western Blotting
IF-IC=Immunofluorescence (Immunocytochemistry)
F=Flow Cytometry
Reactivity Key:
M=Mouse
R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Protocols
- 2442:
- Flow, Immunofluorescence, Western Blotting
Specificity / Sensitivity
HSP27 Antibody (Rodent Preferred) detects endogenous levels of total HSP27 protein. The antibody does not cross-react with other heat shock proteins.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to rat HSP27. Antibodies are purified by protein A and peptide affinity chromatography.
Western Blotting
Western blot analysis of extracts from C2C12, PC12, HeLa and COS cells using HSP27 Antibody (Rodent Preferred).
Flow Cytometry
Flow cytometric analysis of C2C12 cells using HSP27 Antibody (Rodent Preferred) (blue) compared to a nonspecific negative control antibody (red).
IF-IC
Confocal immunofluorescent analysis of C2C12 cells using HSP27 Antibody (Rodent Preferred) (green). Actin filaments have been labeled with Alexa Fluor® 555 phalloidin (red). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).
Background
Heat shock protein (HSP) 27 is one of the small HSPs that are constitutively expressed at different levels in various cell types and tissues. Like other small heat shock proteins, HSP27 is regulated at both the transcriptional and posttranslational levels (1). In response to stress, the expression level of HSP27 increases several-fold to confer cellular resistance to the adverse environmental change. HSP27 is phosphorylated at Ser15, Ser78 and Ser82 by MAPKAP kinase 2 as a result of the activation of the p38 MAP kinase pathway (2,3). Phosphorylation of HSP27 causes a change in its tertiary structure, which shifts from large homotypic multimers to dimers and monomers (4). It has been shown that phosphorylation and increased concentration of HSP27 modulates actin polymerization and reorganization (5,6).
- Arrigo, A.P. and Landry, J. (1994) Cold Spring Harbor Laboratory Press, NY, 335-373.
- Landry, J. et al. (1992) J. Biol. Chem. 267, 794-803.
- Rouse, J. et al. (1994) Cell 78, 1027-1037.
- Rogalla, T. et al. (1999) J. Biol. Chem. 274, 18947-18956.
- Lavoie, J. et al. (1993) J. Biol. Chem. 268, 24210-24214.
- Rousseau, S. et al. (1997) Oncogene 15, 2169-2177.
Application References
Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!
Companion Products
- 2404 Phospho-HSP27 (Ser15) Antibody
- 2405 Phospho-HSP27 (Ser78) Antibody
- 2401 Phospho-HSP27 (Ser82) Antibody
- 2402 HSP27 (G31) Mouse mAb
- 2406 Phospho-HSP27 (Ser82) Antibody II
- 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
This product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.
