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Histone H3, Recombinant, Human

Cat no: H5110-14P

Histone H3, Recombinant, Human

Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the 'beads on a string' structure. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. Acetylation of histone H3 occurs at several different lysine positions in the histone tail and is performed by a family of enzymes known as Histone Acetyl Transferases (HATs). Acetylation of lysine14 is commonly seen in genes that are being actively transcribed into RNA.\n\nQuality Control:\nSDS-PAGE and Coomassie Stain: Purity was assessed by SDS-PAGE and Coomassie blue staining using 1ug of Histone H3.\n\nApplications: \nSuitable for use as a substrate for in vitro enzymatic reactions, such as acetylation by active PCAF (cat# P3114). Other applications not tested.\n\nRecommended Dilutions:\nEnzymatic Assay: Use 0.5-5ug of histone per assay point. Optimal dilutions to be determined by the researcher.\n\nStorage and Stability: Lyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with sterile buffer or ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Reconstituted product is stable for 6 months at -20 degrees 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.

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SPECIFICATIONS

Catalog Number

H5110-14P

Size

100ug

Form

Supplied as a lyophilized powder. Reconstitute in sterile water or buffer.

Purity

Purified by FPLC (Verified by SDS-PAGE)

References

1. Ma, Y., et al., Molecular Endocrinology 24: 76-90 (2010). 2. Saksouk, N., et al., Mol. Cell. Biol., 25: 10301-10314 (2005).

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