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K-Biotin-W-Histone H2B (108-125) (trifluoroacetate salt)

K-Biotin-W-Histone H2B (108-125) (trifluoroacetate salt)
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K-Biotin-W-Histone H2B (108-125) (trifluoroacetate salt)

Catalog No. T36577
Histone H2B (108-125) is a peptide fragment of histone H2B that corresponds to amino acid residues 109-126 of the human histone H2B sequence. It contains an N-terminal biotinylated lysine followed by a tryptophan linker. Histone H2B can be modified by addition of an O-linked N-acetylglucosamine (GlcNAc) moiety to the serine residue at position 112, which promotes monoubiquitination of the lysine at position 120.1 Both of these modifications are associated with active transcription. Histone H2B also has lysine residues at positions 108, 116, and 120 that are subject to acetylation.2
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Product Introduction

Bioactivity
Description
Histone H2B (108-125) is a peptide fragment of histone H2B that corresponds to amino acid residues 109-126 of the human histone H2B sequence. It contains an N-terminal biotinylated lysine followed by a tryptophan linker. Histone H2B can be modified by addition of an O-linked N-acetylglucosamine (GlcNAc) moiety to the serine residue at position 112, which promotes monoubiquitination of the lysine at position 120.1 Both of these modifications are associated with active transcription. Histone H2B also has lysine residues at positions 108, 116, and 120 that are subject to acetylation.2References1. Fujiki, R., Hashiba, W., Sekine, H., et al. GlcNAcylation of histone H2B facilitates its monoubiquitination. Nature 480(7378), 557-560 (2011).2. Portela, A., and Esteller, M. Epigenetic modifications and human disease. Nat. Biotechnol. 28(10), 1057-1068 (2010).
Histone H2B (108-125) is a peptide fragment of histone H2B that corresponds to amino acid residues 109-126 of the human histone H2B sequence. It contains an N-terminal biotinylated lysine followed by a tryptophan linker. Histone H2B can be modified by addition of an O-linked N-acetylglucosamine (GlcNAc) moiety to the serine residue at position 112, which promotes monoubiquitination of the lysine at position 120.1 Both of these modifications are associated with active transcription. Histone H2B also has lysine residues at positions 108, 116, and 120 that are subject to acetylation.2
References1. Fujiki, R., Hashiba, W., Sekine, H., et al. GlcNAcylation of histone H2B facilitates its monoubiquitination. Nature 480(7378), 557-560 (2011).2. Portela, A., and Esteller, M. Epigenetic modifications and human disease. Nat. Biotechnol. 28(10), 1057-1068 (2010).
AliasK-Biotin-W-Histone H2B (108-125) (trifluoroacetate salt)
Chemical Properties
Cas No.
Storage & Solubility Information
StoragePowder: -20°C for 3 years | In solvent: -80°C for 1 year
Solubility Information
H2O: 1 mg/mL

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