Histone H3 combines with Histone H4 to form the H3/H4 tetramer. Because the histones are folded with their subunit partners, the tetramer may be a better substrate for specific enzymes and modifications.
Highly pure, recombinant proteins
Mass confirmed by ESI-TOF MS
Tested for exonuclease, endonuclease and protease contamination
Histone H3.1 combines with Histone H4 to form the H3/H4 tetramer. Two H2A/H2B heterodimers interact with an H3/H4 tetramer to form the histone octamer. Histone H3.1, an H3 variant that has thus far only been found in mammals, is replication dependent and is associated with gene activation and gene silencing. The tetramer is also modified by various enzymes and can act as a substrate for them. These modifications have been shown to be important in gene regulation. Because the histones are folded with their subunit partners, the tetramer may be a better substrate for specific enzymes and modifications.
10 μM, 0.53 mg/ml is calculated using the molar extinction coefficient for Histone H3.1/H4 Tetramer (21,360) and its absorbance at 280 nm (5,6)
To use as a substrate in an enzyme modification assay or other salt sensitive protocol, use 1 to 2 µl of the tetramer in a minimum 20 µl reaction so that the salt concentration in the reaction is ≤ 200 mM.
Because of high salt, the solution does not always remain frozen.
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