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

PathScan® Di-Methyl-Histone H3 (Lys4) Sandwich ELISA Kit #7124

Filter:
  • ELISA

    Supporting Data

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

    Product Information

    Product Description

    The PathScan® Di-Methyl-Histone H3 (Lys4) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of histone H3 when di-methylated at Lys4. A total histone H3 rabbit monoclonal antibody has been coated onto the microwells. After incubation with cell lysates, total histone H3 is captured by the coated antibody. Following extensive washing, biotinylated di-methyl histone H3(lys4) antibody is added to detect the di-methyl Histone H3 (Lys4) protein. HRP-linked streptavidin is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of histone H3 di-methylated at Lys4.

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

    Protocol

    Specificity / Sensitivity

    CST's PathScan® Di-Methyl-Histone H3 (Lys4) Sandwich ELISA Kit #7124 detects endogenous levels of histone H3 when di-methylated at Lys4. As shown in Figure 1, using the Di-Methyl-Histone H3 (Lys4) Sandwich ELISA Kit #7124, a high level of di-methylation at Lys4 on histone H3 is detected in COS cells when treated with TSA. The level of total histone H3 (modified and unmodified) remains unchanged as shown by Western analysis (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

    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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    U.S. Patent No. 7,429,487, foreign equivalents, and child patents deriving therefrom.
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