Human Phospho-HSP27 (S78/S82) Antibody
Human Phospho-HSP27 (S78/S82) Antibody Summary
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Phospho-HSP27 (S78/S82) in HeLa Human Cell Line. HSP27 phosphorylated at S78/S82 was detected in immersion fixed HeLa human cervical epithelial carcinoma cell line unstimulated (lower panel) or stimulated with 20 mJ/cm2ultraviolet radiation (upper panel) using Rabbit Anti-Human Phospho-HSP27 (S78/S82) Monoclonal Antibody (Catalog # MAB23141) at a 10 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Rabbit IgG Secondary Antibody (red; Catalog # NL004) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm and nuclei. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.
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Preparation and Storage
Background: HSP27
Heat shock proteins (HSPs) are a family of highly conserved stress response proteins. Heat shock proteins function primarily as molecular chaperones by facilitating the folding of other cellular proteins, preventing protein aggregation or targeting improperly folded proteins to specific degradative pathways. HSPs are typically expressed at low levels under normal physiological conditions but are dramatically up-regulated in response to cellular stress. Elevated levels of HSPs have been observed in association with ischemia/reperfusion, cancer, and chronic heart failure. HSP27 is a member of the small heat shock protein family, which also includes HSP25 and the alpha -crystallins. Ser78 and Ser82 of HSP27 are phosphorylated in vivo in response to growth factors or heat shock, and the extent of phosphorylation plays a role in determining specific functions. HSP27 forms a large oligomer and functions as an anti-apoptotic molecule, regulating apoptosis through direct interaction with key components of the apoptotic pathway. HSP27 binds and sequesters cytochrome c released from the mitochondria in response to an apoptotic stimulus. This prevents the proper assembly of the apoptosome and subsequently, the activation of procaspase-9 and procaspase-3.
- Gusev, N.B. et al. (2002) Biochemistry (Moscow) 67:511.
- Garrido, C. et al. (2001) Biochem. Biophys. Res. Commun. 286:433.
- Garrido, C. (2002) Cell Death Diffr. 9:483.
- Brvey, J-M. et al. (2000) Nat. Cell Biol. 2:645.
Product Datasheets
Citations for Human Phospho-HSP27 (S78/S82) Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Cellular stress induces non-canonical activation of the receptor tyrosine kinase EphA2 through the p38-MK2-RSK signaling pathway
Authors: Yue Zhou, Ryota Oki, Akihiro Tanaka, Leixin Song, Atsushi Takashima, Naru Hamada et al.
Journal of Biological Chemistry
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Phosphorylated heat shock protein 27 as a potential biomarker to predict the role of chemotherapy-induced autophagy in osteosarcoma response to therapy
Authors: JM Santiago-O, ES Kleinerman, MG Hollomon, A Livingston, WL Wang, JW Tsai, NB Gordon
Oncotarget, 2017-08-17;9(2):1602-1616.
Species: Human
Sample Types: Cell Lysates
Applications: Western Blot
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