| 货号 | 7152C |
| 描述 | CSTs PathScan® Phospho-HSP27 (Ser82) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of phospho-HSP27 (Ser82) protein. An Hsp27 Mouse mAb has been coated onto the microwells. After incubation with cell lysates, HSP27 protein is captured by the coated antibody. Following extensive washing, Phospho-HSP27 (Ser82) Rabbit Antibody is added to detect the captured phospho-HSP27 (Ser82) protein. Anti-rabbit IgG, HRP-linked Antibody #7074 is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of phospho-HSP27 (Ser82) protein. |
| 反应种属 | Human |
| 应用 | ELISA |
| 目标/特异性 | CSTs PathScan® Phospho-HSP27 (Ser82) Sandwich ELISA Kit detects endogenous levels of phospho-HSP27 (Ser82) protein. Using this Sandwich ELISA Kit #7152, a significant induction of phospho-HSP27 (Ser82) can be detected in HeLa cells treated with UV light. This kit detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species. |
| 供应商 | CST |
| 背景 | 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 heat shock proteins, HSP27 is regulated at both the transcriptional and posttranslational levels (1). In response to stress, the expression level of HSP27 increases several-fold to confer cellular resistance to the adverse environmental change. HSP27 is phosphorylated at Ser15, Ser78 and Ser82 by MAPKAP kinase 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). |
| 存放说明 | 4C |
| 参考文献 | Arrigo, A.P. and Landry, J. (1994) Cold Spring Harbor Laboratory Press, NY, 335-373. Landry, J. et al. (1992) J. Biol. Chem. 267, 794-803. Rouse, J. et al. (1994) Cell 78, 1027-1037. Rogalla, T. et al. (1999) J. Biol. Chem. 274, 18947-18956. Lavoie, J. et al. (1993) J. Biol. Chem. 268, 24210-24214. Rousseau, S. et al. (1997) Oncogene 15, 2169-2177. |
Figure 1: Treatment of HeLa cells with UV light stimulates phosphorylation of HSP27 at Ser82 detected by PathScan® Phospho-HSP27 (Ser82) Sandwich ELISA Kit #7152. The corresponding Western blots, using Phospho-HSP27 (Ser82) Antibody #2401 (left) or HSP27 (G31) Mouse mAb #2402 (right), are also shown. 图1：紫外光处理后的HeLa细胞导致HSP27的Ser82磷酸化，可被PathScan Phospho-HSP27 (Ser82) Sandwich ELISA kit #7152所检测到，左图使用Phospho-HSP27 (Ser82) Antibody #2401进行的Western blot，右图为使用HSP27 (G31) Monoclonal Antibody #2402进行的Western blot。 | |
Figure 2: The relationship between protein concentration of lysates from UV-treated or untreated HeLa cells and kit assay optical density readings. HeLa cells (70-85% confluent) were treated with UV light and lysed after incubation at 37C for 20 minutes. |
