p-HSP 27 Antibody (D-3): sc-166694

p-HSP 27 Antibody (D-3) is a mouse monoclonal IgG2b antibody that detects HSP 27 in mouse, rat, and human samples through various applications including western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry with paraffin-embedded sections (IHCP), and enzyme-linked immunosorbent assay (ELISA). anti-HSP 27 antibody (D-3) specifically recognizes the phosphorylated form of HSP 27, a critical heat shock protein that plays a vital role in cellular stress responses. HSP 27 is primarily located in the cytoplasm but translocates to the nucleus under stress conditions, which is essential for its function in protecting cells from apoptosis and promoting cell survival during metabolic stress. HSP 27′s ability to relocate to the nucleus highlights its importance in regulating cellular responses to stress, as HSP 27 can influence gene expression and cellular repair mechanisms. Additionally, HSP 27 undergoes post-translational modifications, including phosphorylation at specific serine residues, which are crucial for activity and interaction with other proteins. For instance, phosphorylation at Serine 15, Serine 78, and Serine 82 enhances chaperone activity and promotes the formation of protein complexes that are vital for cellular protection. HSP 27 monoclonal antibody (D-3) is an invaluable tool for researchers studying the role of HSP 27 in stress response pathways and its implications in various diseases, including cancer and neurodegenerative disorders.

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p-HSP 27 Antibody (D-3) References:

1. TNF-alpha decreases hsp 27 in human blood mononuclear cells: involvement of protein kinase c.  |  Niwa, M., et al. 2006. Life Sci. 80: 181-6. PMID: 17069861
2. Vascular endothelial growth factor induces heat shock protein (HSP) 27 serine 82 phosphorylation and endothelial tubulogenesis via protein kinase D and independent of p38 kinase.  |  Evans, IM., et al. 2008. Cell Signal. 20: 1375-84. PMID: 18440775
3. Diminished phosphorylation of a heat shock protein (HSP 27) in infant acute lymphoblastic leukemia.  |  Strahler, JR., et al. 1991. Biochem Biophys Res Commun. 175: 134-42. PMID: 1998499
4. Hsp-27 induction requires POU4F2/Brn-3b TF in doxorubicin-treated breast cancer cells, whereas phosphorylation alters its cellular localisation following drug treatment.  |  Fujita, R., et al. 2011. Cell Stress Chaperones. 16: 427-39. PMID: 21279488
5. Heat shock proteins in the brain: role of Hsp70, Hsp 27, and HO-1 (Hsp32) and their therapeutic potential.  |  Sharp, FR., et al. 2013. Transl Stroke Res. 4: 685-92. PMID: 24323422
6. Palytoxin induces dissociation of HSP 27 oligomers through a p38 protein kinase pathway.  |  Berni, C., et al. 2015. Chem Res Toxicol. 28: 752-64. PMID: 25710824
7. Hsp-27 and NF-κB pathway is associated with AR/AR-V7 expression in prostate cancer cells.  |  Kiliccioglu, I., et al. 2019. Gene. 697: 138-143. PMID: 30807779
8. Geranylgeranylacetone attenuates cerebral ischemia-reperfusion injury in rats through the augmentation of HSP 27 phosphorylation: a preliminary study.  |  Matsuo, K., et al. 2021. BMC Neurosci. 22: 9. PMID: 33557752
9. Interleukin (IL)-6 signaling leads to phosphorylation of the small heat shock protein (Hsp)27 through activation of the MAP kinase and MAPKAP kinase 2 pathway in monocytes and monocytic leukemia cells.  |  Belka, C., et al. 1995. Leukemia. 9: 288-94. PMID: 7869766
10. A role for the p38 mitogen-activated protein kinase/Hsp 27 pathway in cholecystokinin-induced changes in the actin cytoskeleton in rat pancreatic acini.  |  Schäfer, C., et al. 1998. J Biol Chem. 273: 24173-80. PMID: 9727040

The preferred HSP 27 antibody is HSP 27 Antibody (F-4): sc-13132.