Peptide mixture containing amino acid resides 1-5 and 81-96 of histone H2A
Formulation:
This antibody is provided in phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide and 50% glycerol.
Preparation:
The antibody was purified by antigen-affinity chromatography.
Storage & Handling:
Upon receipt, store frozen at -20° C.
Application:
WB
Recommended Usage:
Each lot of this antibody is quality control tested by Western blotting. Western blotting, suggested working dilution(s): Use 10 μl per 5 ml antibody dilution buffer for each mini-gel. It is recommended that the reagent be titrated for optimal performance for each application.
Jurkat cell extract was resolved by electrophoresis, transferred to nitrocellulose, and probed with rabbit anti-Histone H2A polyclonal antibody. Proteins were visualized using a donkey anti-rabbit secondary conjugated to HRP and a chemiluminescence detection system.
Description:
Histone H2A is a 14 kD nuclear protein that is a component of an octamer containing pairs of each of four core histones (H2A, H2B, H3, H4). The core histones create nucleosome structure of chromosomal fiber in eukaryotes and are dynamic in gene regulation. The histones exhibit cell cycle-dependent transcriptional regulation. Histone H2A can be modified by phosphorylation and acetylation; phosphorylation of H2A correlates with mitotic chromosome condensation. Histone H2A interacts with Histones H3B, H3, and H4 as well as HIV-1 Tat peptides. The Poly6194 antibody has been shown to be useful for the Western blotting of human histone 2A.
Other Names:
Structure:
14 kD basal histone
Distribution:
Nuclear
Function:
Component of octamer containing pairs of each of four core histones (H2A, H2B, H3, H4). Creates nucleosome structure of chromosomal fiber in eukaryotes; dynamic gene regulation
Regulation:
Phosphorylation of H2A correlates with mitotic chromosome condenstion
Modification:
Phosphorylation, acetylation, ubiquitination
Interaction:
Histones H2B, H3, and H4 interact; HIV-1 Tat peptides bind
Antigen References:
1. McGhee, J.D., et al. 1980. Ann. Rev. Biochem. 49:1115. 2. Nakamura, T.M., et al. 2004. Mol. Cell. Biol. 24:6215. 3. Benedetti, A., et al. 2002. Biochem. J. 367:505.
