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Applications: Substrate for histone methyltransferase or acetyltransferase assays. Ideal for screening small molecular inhibitors of histone methyltransferases and acetyltransferases for drug discovery and HTS applications.
Background: The histone octamer is composed of a central heterotetramer of two copies of both histones H3 and H4, flanked by two heterodimers of histones H2A and H2B. The octamer assembles when the H3/H4 tetramer complexes with two H2A/H2B dimers. These histones of the histone octamer all contain N-terminal tails that emanate from their central histone folds and are targets for epigenetic modification.
Description: Human recombinant histone octamer consisting of 2 molecules each of N-terminal His-tagged histones H2A (a.a. 2-130(end)), H2B (a.a. 2-126(end)), H3 (a.a. 2-137(end)), and H4 (a.a. 2-103(end)), expressed in an E. coli expression system. GenBank Accession Nos. are NM_033445, NM_003528, NM_003532, and NM_003548, respectively. H2B has been biotin-labeled via thiol modification of an additional C-terminal cysteine prior to assembly. Global MW = 117 kDa.
Format: Aqueous buffer solution
Formulation: 45 mM Tris pH 7.5, 2 M NaCl, and 10% glycerol.
Genbank: NM_033445, NM_003528, NM_003532, and NM_003548
Host Cell Line: E. coli
Storage Stability: At least 6 months at -80°C.
Tags: N-terminal His-tag, Biotin
Uniprot: Q7L7L0, Q16778, P68431, P62805
Warnings: Avoid freeze/thaw cycles.
Biosafety Level: Not applicable (BSL-1)
References: 1. Miller KM, Jackson SP. Biochem Soc Trans 40(2):370-6 (2012).
2. Raut VV, Pandey SM, Sainis JK. Ann Bot 108(7):1235-46 (2011).
3. Park K, Fasman GD. Biochemistry. 1987 Dec 15;26(25):8042-5.
4. Meagher, R.B., Mussar, K.J., Epigenetics Chromatin 2012 Jul 20,5(1):11.
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