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PDP - Template Name: Antibody Duet
PDP - Template ID: *******ad0fa02

PhosphoPlus® Histone H3 (Ser10) Antibody Duet #12201

PhosphoPlus® Histone H3 (Ser10) Antibody Duet: Image 1
Western blot analysis of extracts from HeLa cells, either untreated or treated with nocodazole (100 ng/ml for 18 hours), using Phospho-Histone H3 (Ser10) (D2C8) XP® Rabbit mAb #3377 (upper) or Histone H3 Antibody #9715 (lower). Phospho-specificity of the antibody is shown by further treatment of the lysate with λ phosphatase.

To Purchase # 12201

Cat. # Size Qty. Price Ships
12201S 1 Kit
$706
  • Product Includes
  • Related Products
Product IncludesQuantityReactivityMW(kDa)Isotype
Phospho-Histone H3 (Ser10) (D2C8) XP® Rabbit mAb #3377100 µlH M R Mk Z17Rabbit IgG
Histone H3 (D1H2) XP® Rabbit mAb #4499100 µlH M R Mk17Rabbit IgG

Product Information

Product Description

PhosphoPlus® Duets from Cell Signaling Technology (CST) provide a means to assess protein activation status. Each Duet contains an activation-state and total protein antibody to your target of interest. These antibodies have been carefully selected to provide superior performance in specified applications.

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).
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