Product Pathways - MAPK Signaling
HSP27 (G31) Mouse mAb #2402
|2402S||100 µl (10 western blots)||---||In Stock||---|
|2402||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Monkey||Endogenous||27||Mouse IgG1|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IHC-P=Immunohistochemistry (Paraffin), IF-IC=Immunofluorescence (Immunocytochemistry)
Specificity / Sensitivity
HSP27 (G31) Mouse mAb detects endogenous levels of total HSP27 protein. The antibody does not cross-react with other heat shock proteins.
Source / Purification
Monoclonal antibody is produced by immunizing animals with full length HSP27 protein.
Western blot analysis of extracts from HeLa and COS-7 cells using HSP27 (G31) Mouse mAb.
Western blot analysis of extracts from HeLa cells, transfected with 100 nM SignalSilence® Control siRNA (Fluorescein Conjugate) #6201 (-) or SignalSilence® HSP27 siRNA I (+) using HSP27 (G31) Mouse mAb and p44/42 MAPK (Erk1/2) (3A7) Mouse mAb #9107. The HSP27 (G31) Mouse mAb confirms silencing of HSP27 expression, while the p44/42 MAPK (Erk1/2) (3A7) Mouse mAb is used to control for loading and specificity of HSP27 siRNA.
Immunohistochemical analysis of paraffin-embedded human lung carcinoma, using HSP27 (G31) Mouse mAb.
Immunohistochemical analysis of paraffin-embedded human breast carcinoma, untreated (left panels) or lambda phosphatase-treated (right panels), using Phospho-HSP27 (Ser82) Antibody #2401 (upper panels) or HSP27 (G31) Mouse mAb (lower panels).
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.
- Sarkar, D. et al. (2002) . Proc. Natl. Acad. Sci. USA 99, 10054-10059. Applications: Western Blotting.
- Kennett, S. B. et al. (2004) J. Biol. Chem. 279, 3300-3307. Applications: Western Blotting.
- Slotta-Huspenina, J. et al. (2012) PLoS One 7, e41420. Applications: Western Blotting, IHC-P (paraffin).
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For Research Use Only. Not For Use In Diagnostic Procedures.
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