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Anti-Histone H4K20me2 (di methyl Lys20) Mouse Antibody [N24L23]

Catalog No.: F3925

Application: Reactivity: Human, Mouse

Usage Information

Dilution
WB1:1000-1:10000 IP1:100-1:500 IF1:100-1:1000

Application
WB, IP, IF

Reactivity
Human, Mouse

Source
Mouse

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

Datasheet & SDS

Biological Description

Specificity
Anti-Histone H4K20me2 (di methyl Lys20) Mouse Antibody [N24L23] recognizes total endogenous levels of Histone H4K20me2 protein, only upon dimethylation at Lys20.

Clone
N24L23

Synonym(s)
Histone H4, H4C1, H4/A, H4FA, HIST1H4A, H4C2, H4/I, H4FI, HIST1H4B, H4C3, H4/G, H4FG, HIST1H4C, H4C4, HIST1H4D, H4C5, H4/J, H4FJ, HIST1H4E

Background
The nucleosome, consisting of four core histone proteins (H2A, H2B, H3, and H4), serves as the fundamental structural unit of chromatin. Once regarded merely as a static scaffold for DNA compaction, histones are now recognized as dynamic regulators, undergoing diverse post-translational modifications such as acetylation, phosphorylation, methylation, and ubiquitination. Among these, histone methylation is particularly critical, as it governs the establishment of active and repressive chromatin states and plays an essential role in genome programming during development. Arginine methylation on histones H3 (Arg2, Arg17, Arg26) and H4 (Arg3) promotes transcriptional activation, catalyzed by protein arginine methyltransferases (PRMTs), including the transcriptional co-activators PRMT1 and CARM1 (PRMT4). H4K20 di- and tri-methylation are preceded by an initial monomethylation step. This modification is catalyzed by KMT5A, a SET-domain–containing methyltransferase. KMT5A shows a strong preference for the intact nucleosome as its substrate, rather than isolated H4 histones or peptides, and carries out H4K20 monomethylation through interactions with H2A and H2B. Histone H4 is dimethylated on lysine 20. H4K20 dimethylation (H4K20me2) is most enriched in the G1 phase, but its levels are reduced by half during S phase due to the incorporation of newly synthesized, unmodified histones into replicating DNA. During G2 phase, H4K20me2 levels are replenished through the activity of KMT5A. The transient reduction of H4K20me2 in S phase is thought to influence the selection of DNA repair pathways, while its restoration in G2 correlates with the formation of 53BP1 nuclear foci.

Background

The nucleosome, consisting of four core histone proteins (H2A, H2B, H3, and H4), serves as the fundamental structural unit of chromatin. Once regarded merely as a static scaffold for DNA compaction, histones are now recognized as dynamic regulators, undergoing diverse post-translational modifications such as acetylation, phosphorylation, methylation, and ubiquitination. Among these, histone methylation is particularly critical, as it governs the establishment of active and repressive chromatin states and plays an essential role in genome programming during development. Arginine methylation on histones H3 (Arg2, Arg17, Arg26) and H4 (Arg3) promotes transcriptional activation, catalyzed by protein arginine methyltransferases (PRMTs), including the transcriptional co-activators PRMT1 and CARM1 (PRMT4). H4K20 di- and tri-methylation are preceded by an initial monomethylation step. This modification is catalyzed by KMT5A, a SET-domain–containing methyltransferase. KMT5A shows a strong preference for the intact nucleosome as its substrate, rather than isolated H4 histones or peptides, and carries out H4K20 monomethylation through interactions with H2A and H2B. Histone H4 is dimethylated on lysine 20. H4K20 dimethylation (H4K20me2) is most enriched in the G1 phase, but its levels are reduced by half during S phase due to the incorporation of newly synthesized, unmodified histones into replicating DNA. During G2 phase, H4K20me2 levels are replenished through the activity of KMT5A. The transient reduction of H4K20me2 in S phase is thought to influence the selection of DNA repair pathways, while its restoration in G2 correlates with the formation of 53BP1 nuclear foci.

References
https://pubmed.ncbi.nlm.nih.gov/29858375/

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

Tech Support

Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

Handling Instructions

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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%