Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. Human Histone H3.1 is intronless and encodes a member of the histone H3 family. Various posttranslational modifications on Histone 3, such as Histone methylation, acetylation, propionylation, butyrylation, formylation, phosphorylation, uniquitylation, sumoylation, citrillination, proline isomerization and ADP ribosylation play an important role for Epigenomic regulation.

Full-length recombinant human Histone H3.1 was constructed with codon optimization and expressed in N-terminal T7-His-TEV cleavage site fusion Tag (29aa) form. This protein was expressed in E. coli as inclusion bodies, refolded using our unique “temperature shift inclusion body refolding” technology and chromatographically purified. Being refolded from inclusion body, this recombinant Histone H3.1 protein does not have any post-translational modification. It may serves as an excellent substrate histone protein for various enzymatic function assays.

1. As native, soluble and non-modified human Histone protein, may be used as specific substrate for enzymatic assays, such as methylation and phosphorylation, et al.

2. May be used as antigen for specific antibody production.

1. Purity: > 90% by SDS-PAGE.

2. Functional Test: Not tested yet.