4 (diMe-Lys26, pSer27) specifically recognizes human histone H1.
Immunogen
dimethylated and phosphorylated synthetic peptide corresponding to amino acids 22-33 (diMe-Lys26, pSer27) of human histone H1.4.
Application
Anti-dimethyl, phospho-Histone H1.4 (diMe-Lys26, pSer27) antibody produced in rabbit is suitable for western blotting at a concentration of 0.5-1μg/mL using acid-extracted fraction of HL60 cells.
Biochem/physiol Actions
The building block of chromatin is the nucleosome which is comprised of an octamer of core histones (H2A, H2B, H3, and H4) around which 147 bp of DNA are wrapped. In mammalian cells, four histone H1 variants (H1.2 to H1.5) are present in all somatic cells, and a fifth (H1.1) is restricted to thymus, testis, and spleen and possibly lymphocytic and neuronal cells. Histone H1.4 is di-methylated or acetylated at Lys26. Lys26 is located within the flexible N-terminal domain of H1.4, just preceding the globular domain.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Storage and Stability
For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing, or storage in “frost-free” freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Genes encoding linker histone variants have evolved to link their expression to signals controlling the proliferative capacities of cells, i.e. cycling and growth-arrested cells express distinct and specific H1 subtypes. In metazoan, these variants show a tripartite structure, with considerably
Current opinion in cell biology, 13(3), 263-273 (2001-05-10)
Post-translational addition of methyl groups to the amino-terminal tails of histone proteins was discovered more than three decades ago. Only now, however, is the biological significance of lysine and arginine methylation of histone tails being elucidated. Recent findings indicate that
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