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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.
COA:
Enter Lot#:
Application References:
1. Peng DJ, et al. 2011. J. Immunol. 186:5638. PubMed.
Hela cell nuclear extract was resolved by electrophoresis, transferred to nitrocellulose, and probed with rabbit anti-histone H3 antibody. Proteins were visualized using a donkey anti-rabbit secondary conjugated to HRP and a chemiluminescence detection system.
Histone H3 is a 17 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 except for the variant H3.3 which is cell cycle-independent. Histone H3 can be modified by phosphorylation, acetylation, ubiquitination, ribosylation, and methylation. Histone H3 has been shown to interact with Rsk-2, MSK1, GCN5 family of HATs, HDACs, PARP, SET7/9, and CARM1. The Poly6019 antibody has been shown to be useful for Western blotting of human and mouse histone H3.
Other Names:
H3.3A, H3F3, H3.3B
Structure:
17 kD
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:
Cell cycle-dependent transcriptional regulation except for variant H3.3, cell cycle-independent
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This data display is provided for general comparisons between formats. Your actual data may vary due to variations in samples, target cells, instruments and their settings, staining conditions, and other factors. If you need assistance with selecting the best format contact our expert technical support team.
Purified anti-Histone H3
Hela cell nuclear extract was resolved by electrophoresis, transferred to nitrocellulose, and probed with rabbit anti-histone H3 antibody. Proteins were visualized using a donkey anti-rabbit secondary conjugated to HRP and a chemiluminescence detection system.