Histone H3 Phospho (pT11) (HIST1H3J) antibody RabMAb®

Cat.#: 5506-1
Abcam ID: ab133457

Rabbit Monoclonal Antibody

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Bulk and Custom formulation available Email request

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Description

Changes in chromatin structure play a large role in the regulation of transcription in eukaryotes (1). The nucleosome is the primary building block of chromatin, and is made up of four core histone proteins (H2A, H2B, H3 and H4) (2). Acetylation of core histones regulates gene expression (2). Histone H3 is primarily acetylated at lysines 9, 14, 18, and 23 (3,4). Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms (3,4). Phosphorylation at Threonine 11 occurs preferentially at the centromere from prophase to anaphase (5).

Recommended Applications

WB

Applications and Recommended Dilution Factors

WB: 1:1,000 - 5,000

Species Reactivity *

Human, Rat

*Species cross-reactivity is based on WB analysis.

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Products Data

Western blot analysis on HeLa cell lysates using anti-Phospho-Histone H3 (pT11) RabMAb (cat. #5506-1). Cells were either (A) untreated (B) treated with FBS and Calyculin A.

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Specificity

A phospho specific peptide corresponding to residues surrounding Threonine 11 of human Histone H3 was used as an immunogen. This antibody only detects Histone H3 phosphorylated at Theronine 11.

Storage Condition and Buffer

Store at -20° C. Buffer: Antibody buffer, sodium azide, glycerol, and BSA. Stable for 12 months from date of receipt.

Alternative Names

HIST1H3J antibody, H3/j antibody, H3FJ antibody, Histone H3.1 antibody, Histone H3/a antibody, Histone H3/b antibody, Histone H3/c antibody, Histone H3/d antibody, Histone H3/f antibody, Histone H3/h antibody, Histone H3/i antibody, Histone H3/j antibody, Histone H3/k antibody, Histone H3/l antibody

Description References

1. Braunstein, M., et al. Mol. Cell. Biol. 16: 4349–56 (1996).
2. Workman, J.L. and R.E. Kingston. Annu. Rev. Biochem. 67: 545–579 (1998).
3. Hansen, J.C. et al. Biochemistry 37, 17637–17641 (1998).
4. Strahl, B.D. and C.D. Allis. Nature 403, 41–45 (2000).
5. Kurihara D et al. BMC Plant Biol. 2011 Apr 28;11:73.

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