Human recombinant histone octamer consisting of 2 molecules each of 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. Each histone protein has an N-terminal His-tag. Global MW = 113.8 kDa.
Host cell line: E. coli
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.
Tag
N-terminal His-tag
Formulation
10 mM Tris pH 7.4, 2 M NaCl, 1 mM EDTA, 5 mM BME, and 10% glycerol
Species
Human
Application
Substrate for histone methyltransferase or acetyltransferase assays. Ideal for screening small molecular inhibitors of histone methyltransferases and acetyltransferases for drug discovery and HTS applications. Since the recombinant histone proteins in thi
Notes
Avoid freeze/thaw cycles.
GenBank
NM_033445, NM_003528, NM_003532, NM_003548
Mw(kda)
116 kDa
Uniprot
Q7L7L0, Q16778, P68431, P62805
Shipping Temperature
-80°C (dry ice)
Format
Aqueous buffer solution
Storage
Stable at -80°C for at least 6 months from date of receipt, when stored as directed
Reference
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.