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Render Timestamp: 2024-12-09T11:56:19.384Z
Commit: 224419269841c11382c4555dbee545259bf6c379
XML generation date: 2024-09-20 06:20:07.006
Product last modified at: 2024-09-19T22:13:07.788Z
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PDP - Template Name: FastScan ELISA Kit
PDP - Template ID: *******a26362b

FastScan Phospho-HSP27 (Ser82) ELISA Kit #15429

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  • ELISA

    Supporting Data

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

    Product Information

    Product Description

    The FastScan™ Phospho-HSP27 (Ser82) ELISA Kit is a sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of HSP27 when phosphorylated at Ser82. To perform the assay, sample is incubated with a capture antibody conjugated with a proprietary tag and a second detection antibody linked to HRP, forming a sandwich with phospho-HSP27 (Ser82) in solution. This entire complex is immobilized to the plate via an anti-tag antibody. The wells are then washed to remove unbound material. TMB is then added. The magnitude of observed signal is proportional to the quantity of phospho-HSP27 (Ser82).

    *Antibodies in this kit are custom formulations specific to kit.

    Protocol

    Specificity / Sensitivity

    The FastScan™ Phospho-HSP27 (Ser82) ELISA Kit detects endogenous levels of HSP27 when phosphorylated at Ser82 as shown in Figure 1. 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, Monkey

    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.
    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
    FastScan™ ELISA is a registered trademark of Cell Signaling Technology, Inc.
    U.S. Patents 9,086,407, 9,261,500, and 9,476,874, foreign equivalents, and child patents deriving therefrom.
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