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PDP - Template Name: ELISA Kit
PDP - Template ID: *******bd382c2

PathScan® Phospho-HSP27 (Ser82) Sandwich ELISA Kit #7152

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  • ELISA

Important Ordering Details

Custom Ordering Details:

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    Supporting Data

    REACTIVITY H
    Application Key:
    • ELISA-ELISA 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Description

    CST's 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 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.

    *Antibodies in kit are custom formulations specific to kit.

    Protocol

    Specificity / Sensitivity

    CST's 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.

    Species Reactivity:

    Human

    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).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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