Product Includes | Product # | Quantity | Color | Storage Temp |
---|---|---|---|---|
HSP27 Rabbit mAb Coated Microwells | 42806 | 96 tests |
|
+4C |
HSP27 Mouse Detection mAb | 14260 | 1 ea |
|
+4C |
Anti-mouse IgG, HRP-linked Antibody (ELISA Formulated) | 13304 | 1 ea |
|
+4C |
Detection Antibody Diluent | 13339 | 11 ml |
|
+4C |
HRP Diluent | 13515 | 11 ml |
|
+4C |
TMB Substrate | 7004 | 11 ml |
|
+4C |
STOP Solution | 7002 | 11 ml |
|
+4C |
Sealing Tape | 54503 | 2 ea |
|
+4C |
ELISA Wash Buffer (20X) | 9801 | 25 ml |
|
+4C |
ELISA Sample Diluent | 11083 | 25 ml |
|
+4C |
Cell Lysis Buffer (10X) | 9803 | 15 ml |
|
-20C |
*The microwell plate is supplied as 12 8-well modules - Each module is designed to break apart for 8 tests.
Description
CST's PathScan® Total HSP27 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of total HSP27 protein. An HSP27 Antibody has been coated onto the microwells. After incubation with cell lysates, both nonphospho- and phospho-HSP27 are captured by the coated antibody. Following extensive washing, an HSP27 Mouse mAb is added to detect the captured HSP27 protein. Anti-mouse IgG, HRP-linked antibody 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 total HSP27 protein.
*Antibodies in kit are custom formulations specific to kit.
Specificity/Sensitivity
Background
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).
Background References
Cross-Reactivity Key
H: human M: mouse R: rat Hm: hamster Mk: monkey Vir: virus Mi: mink C: chicken Dm: D. melanogaster X: Xenopus Z: zebrafish B: bovine Dg: dog Pg: pig Sc: S. cerevisiae Ce: C. elegans Hr: horse GP: Guinea Pig Rab: rabbit All: all species expected
Trademarks and Patents
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