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Render Timestamp: 2024-11-22T10:45:15.376Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-04-05 20:22:11.019
Product last modified at: 2024-06-27T13:36:12.744Z
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PDP - Template Name: Blocking Peptide
PDP - Template ID: *******6db2f4c

Phospho-Histone H3 (Ser10) Blocking Peptide #1000

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    Product Information

    Product Usage Information

    Use as a blocking reagent to evaluate the specificity of antibody reactivity in dot blot protocols.

    Storage

    Supplied in 20 mM potassium phosphate (pH 7.0), 50 mM NaCl, 0.1 mM EDTA, 1 mg/ml BSA, 5% glycerol and 1% DMSO. Store at –20°C.

    Product Description

    This peptide is used to block Phospho-Histone H3 (Ser10) (D2C8) XP Rabbit mAb #3377 reactivity.
    MW (kDa) Formula Weight: 1507.74 grams/mol

    Quality Control

    The quality of the peptide was evaluated by reversed-phase HPLC and by mass spectrometry. The peptide reacts with Phospho-Histone H3 (Ser10) (D2C8) XP #3377 by dot blot.

    Background

    Modulation of chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of DNA wound around eight core histone proteins (two each of H2A, H2B, H3, and H4), is the primary building block of chromatin (1). The amino-terminal tails of core histones undergo various posttranslational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (2-5). These modifications occur in response to various stimuli and have a direct effect on the accessibility of chromatin to transcription factors and, therefore, gene expression (6). In most species, histone H2B is primarily acetylated at Lys5, 12, 15, and 20 (4,7). Histone H3 is primarily acetylated at Lys9, 14, 18, 23, 27, and 56. Acetylation of H3 at Lys9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms (2,3). Phosphorylation at Ser10, Ser28, and Thr11 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis (8-10). Phosphorylation at Thr3 of histone H3 is highly conserved among many species and is catalyzed by the kinase haspin. Immunostaining with phospho-specific antibodies in mammalian cells reveals mitotic phosphorylation at Thr3 of H3 in prophase and its dephosphorylation during anaphase (11).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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