Catalog # M2508 was discontinued on December 18, 2023
Histone H2A combines with Histone H2B to form the H2A/H2B heterodimer. Two H2A/H2B heterodimers interact with an H3/H4 tetramer to form the histone octamer.
Histones are modified by various enzymes and can act as substrates for them. These modifications have been shown to be important in gene regulation. Because the histones are folded with their subunit partners, the dimer may be a better substrate for specific enzymes and modifications.
Highly pure, recombinant protein
Mass confirmed by ESI-TOF MS
Tested for exonuclease, endonuclease and protease contamination
20 mM Tris-HCl
2 M NaCl
1 mM DTT
1 mM EDTA
pH 8 @ 25°C
Molecular Weight
Theoretical: 27779 daltons
Product Notes
20 μM, 0.55 mg/ml is calculated using the molar extinction coefficient for Histone H2A/H2B Dimer (11,920) and its absorbance at 280 nm (4, 5)
To use as a substrate in an enzyme modification assay or other salt sensitive protocol, use 1 to 2 µl of the dimer in a minimum 20 µl reaction so that the salt concentration in the reaction ≤ 200 mM.
Because of high salt, the solution does not always remain frozen.
Gill, S.C. and von Hippel, P.H. (1989). Anal. Biochem. 182, 319-326.
Pace, C.N. et al. (1995). Protein Science. 4, 2411-2423.
FAQs & Troubleshooting
Tech Tips
To use as a substrate in an enzyme modification assay or other salt sensitive protocol, use 1 to 2 μl of the dimer in a minimum 20 μl reaction so that the salt concentration in the reaction = 200 mM.
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