
Sku: WR6514

Catalog No.: WR6510
Specification: 100µg/10µg
Stock: In stock
Product details, specifications, documents, and related products are available from the catalog record. Learn more
Background:AbFlex ® antibodies are recombinant antibodies (rAbs) that have been generated using defined DNA sequences to produce highly specific, reproducible antibodies. Each AbFlex antibody contains a 6xHis Tag, a Biotinylation Tag for enzymatic biotin conjugation using the biotin ligase, BirA, and a sortase recognition motif (LPXTG) to attach a variety of labels directly to the antibody including fluorophores, enzymatic substrates (HRP, AP), peptides, drugs as well as solid supports. AbFlex ® Histone H3.3K27acS31ph antibody was expressed as full-length IgG with mouse immunoglobulin heavy and light chains (IgG2a isotype) in mammalian 293 cells. The antibody was directly labeled with biotin using the biotin ligase, BirA. Histone H4 is one of the core components of the nucleosome. The nucleosome is the smallest subunit of chromatin and consists of 147 base pairs of DNA wrapped around an octamer of core histone proteins (two each of Histone H2A , Histone H2B , Histone H3 and Histone H4 ). Chromatin is subject to a variety of chemical modifications, including post-translational modifications of the histone proteins and the methylation of cytosine residues in the DNA. Reported histone modifications include acetylation, methylation, phosphorylation, ubiquitylation, glycosylation, ADP-ribosylation, carbonylation and SUMOylation; these modifications play a major role in regulating gene expression. One of the histone variants, H3.3, has a difference of 4 to 5 amino acid residues between the sequence variants of H3 (H3.1 and H3.2). TThe only contrasting residue is serine, contained at the N-terminus of the protein at position 31. Ser31 phosphorylation is known as a mitotic epigenetic modification. H3K27ac is also preferentially deposited in H3.3, therefore this H3.3K27acS31ph antibody was developed due to the high likelihood that H3.3 proteins contain the dual modification of both acetylation at lysine residue 27 and phosphorylation at serine residue 31.
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