Histone H3 (di methyl Lys79) Antibody [F10E18]

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:2500 IHC1:2000 IF1:2000 CHIP1:200

Application
WB, IHC, IF, ChIP

Reactivity
Mouse, Rat, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
15 kDa 15 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Human colon tissue; Rat pancreas tissue; Mouse liver tissue; HeLa cells; NIH/3T3 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
Histone H3 (di methyl Lys79) Antibody [F10E18] detects endogenous levels of total Histone H3 protein only when it is di metylated at Lys79.

Clone
F10E18

Background
Histone H3 di-methylated at lysine 79 (H3K79me2) is a post-translational modification occurring on lysine 79 within the globular core of histone H3, a key component of the nucleosome that packages eukaryotic DNA. This dimethylation is catalyzed by the DOT1 methyltransferase, which adds two methyl groups to the ε-amino group of K79, a residue buried within the histone fold domain. The addition of these methyl groups distorts the nucleosomal surface and electrostatically repels the adjacent H3-H4 acidic patch, thereby reducing the affinity between DNA and histone without compromising the stability of the nucleosome as a whole. H3K79me2 is a hallmark of transcriptionally active euchromatin and is instrumental in recruiting DOT1L-interacting readers that maintain an open chromatin structure. This modification works together with H2B ubiquitination to facilitate RNA polymerase II elongation and to suppress cryptic transcription initiation. H3K79me2 is also enriched at replication origins, where it restricts replication fork licensing to a single event per cell cycle through DOT1L-mediated suppression of re-replication origins. Additionally, H3K79me2 influences DNA double-strand break repair pathway choice by favoring homologous recombination over non-homologous end joining through the antagonism of 53BP1 foci formation. Dysregulation of DOT1L and subsequent H3K79me2 elevation is implicated in MLL-rearranged leukemias by driving oncogene expression such as c-Myc, whereas loss of this modification increases sensitivity to replication stress and leads to aberrant replication timing, contributing to cancer pathogenesis.

Background

Histone H3 di-methylated at lysine 79 (H3K79me2) is a post-translational modification occurring on lysine 79 within the globular core of histone H3, a key component of the nucleosome that packages eukaryotic DNA. This dimethylation is catalyzed by the DOT1 methyltransferase, which adds two methyl groups to the ε-amino group of K79, a residue buried within the histone fold domain. The addition of these methyl groups distorts the nucleosomal surface and electrostatically repels the adjacent H3-H4 acidic patch, thereby reducing the affinity between DNA and histone without compromising the stability of the nucleosome as a whole. H3K79me2 is a hallmark of transcriptionally active euchromatin and is instrumental in recruiting DOT1L-interacting readers that maintain an open chromatin structure. This modification works together with H2B ubiquitination to facilitate RNA polymerase II elongation and to suppress cryptic transcription initiation. H3K79me2 is also enriched at replication origins, where it restricts replication fork licensing to a single event per cell cycle through DOT1L-mediated suppression of re-replication origins. Additionally, H3K79me2 influences DNA double-strand break repair pathway choice by favoring homologous recombination over non-homologous end joining through the antagonism of 53BP1 foci formation. Dysregulation of DOT1L and subsequent H3K79me2 elevation is implicated in MLL-rearranged leukemias by driving oncogene expression such as c-Myc, whereas loss of this modification increases sensitivity to replication stress and leads to aberrant replication timing, contributing to cancer pathogenesis.

References
https://pubmed.ncbi.nlm.nih.gov/23754963/ https://pubmed.ncbi.nlm.nih.gov/18794842/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%