Phospho-HSP27 (Ser82) (D1H2F6) XP® Rabbit mAb (BSA and Azide Free) #64293
- WB
- IHC
- IF
- F
Supporting Data
| REACTIVITY | H M |
| SENSITIVITY | Endogenous |
| MW (kDa) | 27 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
- IF-Immunofluorescence
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
Product Information
Product Usage Information
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
Formulation
Storage
Specificity / Sensitivity
Phospho-HSP27 (Ser82) (D1H2F6) XP® Rabbit mAb (BSA and Azide Free) recognizes endogenous levels of HSP27 protein only when phosphorylated at Ser82.
Species Reactivity:
Human, Mouse
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Rat, Hamster, Bovine, Dog, Horse
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser82 of human HSP27 protein.
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 HSPs, HSP27 is regulated at both the transcriptional and posttranslational levels (1). In response to stress, the HSP27 expression increases several-fold to confer cellular resistance to the adverse environmental change. HSP27 is phosphorylated at Ser15, Ser78, and Ser82 by MAPKAPK-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).
- Stetler, R.A. et al. (2009) Curr Mol Med 9, 863-72.
- Landry, J. et al. (1992) J Biol Chem 267, 794-803.
- Rouse, J. et al. (1994) Cell 78, 1027-37.
- Rogalla, T. et al. (1999) J Biol Chem 274, 18947-56.
- Lavoie, J.N. et al. (1993) J Biol Chem 268, 24210-4.
- Rousseau, S. et al. (1997) Oncogene 15, 2169-77.
- Aoyama, A. et al. (1993) Mol Cell Biol 13, 1824-35.
Limited Uses
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