Render Target: SSR
Render Timestamp: 2024-11-21T21:21:29.712Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-08-01 15:25:21.989
Product last modified at: 2024-11-08T16:30:10.017Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-HSP27 (Ser78) Antibody #2405

Filter:
  • WB
  • IHC
  • F

    Supporting Data

    REACTIVITY H Mk
    SENSITIVITY Endogenous
    MW (kDa) 27
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    • IHC-Immunohistochemistry 
    • F-Flow Cytometry 
    Species Cross-Reactivity Key:
    • H-Human 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunohistochemistry (Paraffin) 1:100
    Flow Cytometry (Fixed/Permeabilized) 1:100

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-HSP27 (Ser78) Antibody detects endogenous levels of HSP27 phosphorylated at Ser78 . This antibody does not cross-react with other phosphorylated heat shock proteins.

    Species Reactivity:

    Human, Monkey

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser78 of human HSP27. Antibodies are purified by protein A and peptide affinity chromatography.

    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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