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P hsp27 ser82

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P-Hsp27 (ser82) is a lab equipment product from Cell Signaling Technology. It detects phosphorylation of Hsp27 at serine 82 residue.

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Lab products found in correlation

P p38 thr180 tyr182, by Cell Signaling Technology (2 mentions) Sds page minigels, by Bio-Rad (2 mentions) P38 total h147, by Santa Cruz Biotechnology (2 mentions) β actin, by Merck Group (2 mentions) Bca protein assay kit, by Thermo Fisher Scientific (2 mentions) Protease inhibitor cocktail, by Santa Cruz Biotechnology (1 mentions) Odyssey blocking buffer in pbs, by LI COR (1 mentions) Gapdh, by Merck Group (1 mentions)

Spelling variants of this product

HSP27 (39 citations) P-HSP27 (16 citations)

3 protocols using p hsp27 ser82

1

Hypoxia-induced stress response in viral infection

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Cells were seeded at 1×106 cells/well in 1600ul of medium in 6-well plates in normoxia or hypoxia. The next day, cells were infected at 10 PFU/cell with C101 or C154 for 24 hours. Uninfected cells served as controls. An equal amount of protein (35ug) from each lysate sample was loaded in a well of 4-15% SDS-PAGE mini gels (Bio-Rad, Hercules, CA), electrophoretically separated, transferred to PVG membranes, and immunoblotting was performed as previously described.5 Antibodies used were p38 total (H147; Santa Cruz, Dallas, TX); p-p38 (Thr180/Tyr182; Cell Signaling Technology, Danvers, MA); p-Hsp27 (ser82: Cell Signaling Technology); and β-actin, (Sigma-Aldrich) which was used to confirm equal protein loading.
Friedman G.K., Nan L., Haas M.C., Kelly V.M., Moore B.P., Langford C.P., Xu H., Han X., Beierle E.A., Markert J.M., Cassady K.A, & Gillespie G.Y. (2014). γ134.5-Deleted HSV-1 Expressing Human Cytomegalovirus IRS1 Gene Kills Human Glioblastoma Cells as Efficiently as Wild-type HSV-1 in Normoxia or Hypoxia. Gene therapy, 22(4), 348-355.
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2

Hypoxia-induced stress response in viral infection

Check if the same lab product or an alternative is used in the 5 most similar protocols
Cells were seeded at 1×106 cells/well in 1600ul of medium in 6-well plates in normoxia or hypoxia. The next day, cells were infected at 10 PFU/cell with C101 or C154 for 24 hours. Uninfected cells served as controls. An equal amount of protein (35ug) from each lysate sample was loaded in a well of 4-15% SDS-PAGE mini gels (Bio-Rad, Hercules, CA), electrophoretically separated, transferred to PVG membranes, and immunoblotting was performed as previously described.5 Antibodies used were p38 total (H147; Santa Cruz, Dallas, TX); p-p38 (Thr180/Tyr182; Cell Signaling Technology, Danvers, MA); p-Hsp27 (ser82: Cell Signaling Technology); and β-actin, (Sigma-Aldrich) which was used to confirm equal protein loading.
Friedman G.K., Nan L., Haas M.C., Kelly V.M., Moore B.P., Langford C.P., Xu H., Han X., Beierle E.A., Markert J.M., Cassady K.A, & Gillespie G.Y. (2014). γ134.5-Deleted HSV-1 Expressing Human Cytomegalovirus IRS1 Gene Kills Human Glioblastoma Cells as Efficiently as Wild-type HSV-1 in Normoxia or Hypoxia. Gene therapy, 22(4), 348-355.
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3

Western Blot Analysis Methodology

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Western blots were either performed from total cell lysates obtained by lysing cells directly with RIPA buffer complemented with PMSF, protease inhibitor cocktail and sodium orthovanadate (Santa Cruz, CAT# sc-24948). Proteins concentration was determined using BCA protein assay kit (Thermo). SDS-PAGE electrophoresis was carried out in 7.5% pre-cast polyacrylamide gels (Bio-Rad, CAT# 5671023). After transfer onto nitrocellulose, membranes were blocked for 30 min with Odyssey Blocking Buffer in PBS (Part Number: 927-40000, LI-COR Biosciences) and probed overnight with primary antibody: p-HSP27(Ser 82) (1:500, Cell Signaling, CAT# 9709), p-p38 (1:1000, Cell Signaling, CAT# 9211), p38 (1:1000, Cell Signaling, CAT# 8690), MyHC (1:500, Millipore, CAT# 05-716), GAPDH (1:500, Millipore, CAT# MAB374). After that, IRDye700-conjugated or IRDye800-conjugated secondary antibodies were used and visualized with the Odyssey infrared detector (LI-COR Biosciences, Westburg, Leusden, The Netherlands). For Protein quantification a, we used the background correction option in the software of the supplier (Image Studio™ Software for the Odyssey CLx-LI-COR Biosciences) and scanned the corresponding band of the protein of interest.
Ding S., Swennen G.N., Messmer T., Gagliardi M., Molin D.G., Li C., Zhou G, & Post M.J. (2018). Maintaining bovine satellite cells stemness through p38 pathway. Scientific Reports, 8, 10808.
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