Histone H3, phosphorylated (Ser10) Blocking Peptide

Modulation of the chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of four core histone proteins (H2A, H2B, H3 and H4), is the primary building block of chromatin (1). The N-terminal tail of core histones undergoes different posttranslational modifications including acetylation, phosphorylation and methylation (2–4). These modifications occur in response to cell signal stimuli and have a direct effect on gene expression. In most species, the histone H2B is primarily acetylated at lysines 5, 12, 15 and 20 (4,5). Histone H3 is primarily acetylated at lysines 9, 14, 18 and 23 (2,3). Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms (2,3). Phosphorylation at Ser10 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis (6).

Synthetic phosphopeptide corresponding to residues surrounding serine 10 of human histone H3.

Corresponding antibody, H5110-13J, detects endogenous histone H3 only when phosphorylated at serine 10. It is a useful tool in characterizing histone phosphorylation and in monitoring mitosis and meiosis with immunocytochemistry. Does not crossreact with other phosphorylated histones, or with histone H3 modified by acetylation. Recognizes human, mouse, rat, monkey.

Applications:
Suitable for use in ELISA, Western Blot or for antigen applications in immunological protocols. Other applications not tested.

Recommended Dilution:
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 6 months after receipt at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.