Product Pathways - Protein Folding
PhosphoPlus® HSP27 (Ser82) Antibody Duet #11900
| Duet Includes | Quantity | Applications | Reactivity | MW (kDa) | Isotype |
|---|---|---|---|---|---|
| Phospho-HSP27 (Ser82) (D1H2) XP® Rabbit mAb #9709 | 100 µl | W IHC-P IF-IC F | H M (R) (Hm) (B) (Dg) (Hr) | 27 | Rabbit IgG |
| HSP27 (G31) Mouse mAb #2402 | 100 µl | W IHC-P IF-IC | H Mk | 27 | Mouse IgG1 |
Applications Key:
W=Western Blotting
IHC-P=Immunohistochemistry (Paraffin)
IF-IC=Immunofluorescence (Immunocytochemistry)
F=Flow Cytometry
Reactivity Key:
H=Human
M=Mouse
R=Rat
Hm=Hamster
Mk=Monkey
B=Bovine
Dg=Dog
Hr=Horse
Species in parentheses are predicted to react based on 100% sequence homology.
Protocols
- 2402:
- IHC / Paraffin, Immunofluorescence, Western Blotting
- 9709:
- Flow, IHC / Paraffin, Immunofluorescence, Western Blotting
Description
PhosphoPlus® Duets from Cell Signaling Technology (CST) provide a means to assess protein activation status. Each Duet contains an activation-state and total protein antibody to your target of interest. These antibodies have been selected from CST's product offering based upon superior performance in specified applications.
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).
- 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.
For Research Use Only. Not For Use In Diagnostic Procedures.
