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11900
PhosphoPlus® HSP27 (Ser82) Antibody Duet
Primary Antibodies

PhosphoPlus® HSP27 (Ser82) Antibody Duet #11900

Western Blotting Image 1

Western blot analysis of extracts from HeLa or HT-29 cells, untreated (-) or treated (+) with either UV (40 mJ/cm2 with 30 min recovery) or anisomycin (25 μg/mL, 30 min), using Phospho-HSP27 (Ser82) (D1H2F6) XP® Rabbit mAb.

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Western Blotting Image 2

Western blot analysis of extracts from HeLa and COS-7 cells using HSP27 (G31) Mouse mAb.

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IHC-P (paraffin) Image 3

Immunohistochemical analysis of paraffin-embedded human breast carcinoma, control (left) or λ phosphatase-treated (right), using Phospho-HSP27 (Ser82) (D1H2F6) XP® Rabbit mAb.

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Western Blotting Image 4

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.

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IHC-P (paraffin) Image 5

Immunohistochemical analysis of paraffin-embedded mouse lung using Phospho-HSP27 (Ser82) (D1H2F6) XP® Rabbit mAb.

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IHC-P (paraffin) Image 6

Immunohistochemical analysis of paraffin-embedded human lung carcinoma, using HSP27 (G31) Mouse mAb.

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IHC-P (paraffin) Image 7

Immunohistochemical analysis of paraffin-embedded HeLa cell pellets, control (left) or UV-treated (right), using Phospho-HSP27 (Ser82) (D1H2F6) XP® Rabbit mAb.

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IHC-P (paraffin) Image 8

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).

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IHC-P (paraffin) Image 9

Immunohistochemical analysis of paraffin-embedded human lung carcinoma using Phospho-HSP27 (Ser82) (D1H2F6) XP® Rabbit mAb in the presence of control peptide (left) or antigen-specific peptide (right).

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IF-IC Image 10

Confocal immunofluorescent analysis of A549 cells using HSP27 (G31) Mouse mAb (green). Red = Propidium iodide (fluorescent DNA dye).

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IHC-P (paraffin) Image 11

Immunohistochemical analysis of paraffin-embedded human prostate carcinoma using Phospho-HSP27 (Ser82) (D1H2F6) XP® Rabbit mAb.

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Flow Cytometry Image 12

Flow cytometric analysis of HeLa cells, untreated (blue) or UV-treated (green), using Phospho-HSP27 (Ser82) (D1H2F6) XP® Rabbit mAb.

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IF-IC Image 13

Confocal immunofluorescent analysis of C2C12 cells, untreated (left) or treated with λ phosphatase (middle), and NIH/3T3 cells (right) using Phospho-HSP27 (Ser82) (D1H2F6) XP® Rabbit mAb (green). Actin filaments were labeled with DY-554 phalloidin (red). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye). Negative staining in NIH/3T3 cells is in agreement with the observation that NIH/3T3 cells do not express HSP27 under basal conditions (5,7).

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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Phospho-HSP27 (Ser82) (D1H2F6) XP® Rabbit mAb 9709 100 µl
  • WB
  • IHC
  • IF
  • F
H M 27 Rabbit IgG
HSP27 (G31) Mouse mAb 2402 100 µl
  • WB
  • IHC
  • IF
H Mk 27 Mouse IgG1

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.

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).

  1. Arrigo, A.P. and Landry, J. (1994) Cold Spring Harbor Laboratory Press, NY, 335-373.
  2. Landry, J. et al. (1992) J. Biol. Chem. 267, 794-803.
  3. Rouse, J. et al. (1994) Cell 78, 1027-37.
  4. Rogalla, T. et al. (1999) J. Biol. Chem. 274, 18947-18956.
  5. Lavoie, J. et al. (1993) J. Biol. Chem. 268, 24210-24214.
  6. Rousseau, S. et al. (1997) Oncogene 15, 2169-2177.
Entrez-Gene Id
3315
Swiss-Prot Acc.
P04792
For Research Use Only. Not For Use In Diagnostic Procedures.

Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
PhosphoPlus is a trademark of Cell Signaling Technology, Inc.

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