Detection of Human and Mouse Phospho-HSP27 (S78/S82) by Western Blot.
Western blot shows lysates of HeLa human cervical epithelial carcinoma cell line and C2C12 mouse myoblast cell line untreated (-) or treated (+) with 100 J/m2 UV-C for 30 minutes. PVDF membrane was probed with 0.1 µg/mL of Rabbit Anti-Human/Mouse/Rat Phospho-HSP27 (S78/S82) Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2314), followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # HAF008). A specific band was detected for Phospho-HSP27 (S78/S82) at approximately 27 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
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/cm2 ultraviolet radiation (upper panel) using Rabbit Anti-Human/Mouse/Rat Phospho-HSP27 (S78/S82) Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2314) at 1 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.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
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. HSP27 forms a large oligomer and the extent of phosphorylation plays a role in determining specific functions. HSP27 also 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.
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