Histone H3 (mono methyl Lys27) Antibody [G24J14]

Application: Reactivity: Human, Mouse, Rat, Monkey

Lane 1: Hela, Lane 2: C2C12

Usage Information

Dilution
WB1:1000 IP1:50

Application
WB, IP

Reactivity
Human, Mouse, Rat, Monkey

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
17 kDa

Positive Control	HeLa cells; C2C12 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
Histone H3 (mono methyl Lys27) Antibody [G24J14] recognizes endogenous levels of histone H3 protein only when mono-methylated at Lys27.

Clone
G24J14

Synonym(s)
Histone H3.1; Histone H3/a; Histone H3/b; Histone H3/c; H3C1; H3FA; HIST1H3A; H3C2; H3FL; HIST1H3B; H3C3; H3FC; HIST1H3C; H3C4; H3FB; HIST1H3D; H3C6; H3FD; HIST1H3E; H3C7; H3FI; HIST1H3F; H3C8; H3FH

Background
Histone H3 monomethyl Lys27 (H3K27me1) is a pivotal post-translational modification that adds a methyl group to the ε-amino group of Lys27 on histone H3, a core nucleosomal protein forming octamers with H2A, H2B, and H4 to package DNA. This modification occurs on the flexible N-terminal tail (amino acids 1–40) and the globular histone fold (amino acids 94–123), and is deposited by PRC2/EZH2 (which prefers mono- over tri-methylation) or through SETD2-opposed pathways. H3K27me1 marks permissive, active, or poised chromatin at gene bodies, enhancers, and bivalent promoters during development and differentiation, in contrast to the repressive H3K27me3 mark. The methylated K27 embeds in a hydrophobic H3-H3 interface pocket (modulated by Ala28 and Pro30), can coexist with H3K36me3 to enhance nucleosome mobility and RNA Pol II access (unlike the compact PRC1-bound H3K27me3 state), recruits reader proteins via PHD or Tudor motifs (such as BPTF, but not CBX chromodomains), and is reversible by JMJD3/UTX demethylases (primarily active on di- and tri-methylation, but also on mono-methylation). H3K27me1 drives transcriptional activation and elongation, enhancer-promoter looping, high gene expression, genome programming during embryogenesis and erythroid differentiation, and antagonism of H3K27me3 at lineage-specific loci. Dysregulation of H3K27me1, such as through PRC2 mutations that shift the mono- to tri-methylation balance, underlies cancers (including leukemia and pediatric tumors) and developmental disorders; treatment with EZH2 inhibitors can elevate H3K27me1 and activate tumor suppressor genes.

Background

Histone H3 monomethyl Lys27 (H3K27me1) is a pivotal post-translational modification that adds a methyl group to the ε-amino group of Lys27 on histone H3, a core nucleosomal protein forming octamers with H2A, H2B, and H4 to package DNA. This modification occurs on the flexible N-terminal tail (amino acids 1–40) and the globular histone fold (amino acids 94–123), and is deposited by PRC2/EZH2 (which prefers mono- over tri-methylation) or through SETD2-opposed pathways. H3K27me1 marks permissive, active, or poised chromatin at gene bodies, enhancers, and bivalent promoters during development and differentiation, in contrast to the repressive H3K27me3 mark. The methylated K27 embeds in a hydrophobic H3-H3 interface pocket (modulated by Ala28 and Pro30), can coexist with H3K36me3 to enhance nucleosome mobility and RNA Pol II access (unlike the compact PRC1-bound H3K27me3 state), recruits reader proteins via PHD or Tudor motifs (such as BPTF, but not CBX chromodomains), and is reversible by JMJD3/UTX demethylases (primarily active on di- and tri-methylation, but also on mono-methylation). H3K27me1 drives transcriptional activation and elongation, enhancer-promoter looping, high gene expression, genome programming during embryogenesis and erythroid differentiation, and antagonism of H3K27me3 at lineage-specific loci. Dysregulation of H3K27me1, such as through PRC2 mutations that shift the mono- to tri-methylation balance, underlies cancers (including leukemia and pediatric tumors) and developmental disorders; treatment with EZH2 inhibitors can elevate H3K27me1 and activate tumor suppressor genes.

References
https://pubmed.ncbi.nlm.nih.gov/38959894/ https://www.nature.com/articles/cr201122

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%