Histone H3 (mono methyl K9) Antibody [G13B9]

Application: Reactivity: Mouse, Rat, Human

Lane 1: Hela, Lane 2: NIH/3T3

Usage Information

Dilution
WB1:20000 IHC1:2000 IF1:2000 CHIP1:1000

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. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
Histone H3 (mono methyl K9) Antibody [G13B9] detects endogenous levels of total Histone H3 protein only when it is mono‑methylated at K9.

Clone
G13B9

Synonym(s)
H3FA; HIST1H3A; H3C2; H3FL; HIST1H3B; H3C3; H3FC; HIST1H3C; H3C4; H3FB; HIST1H3D; H3C6; HIST1H3H; H3C11; H3FF; HIST1H3I; H3C12; H3FJ; HIST1H3J; H3C1; Histone H3.1; Histone H3/a; Histone H3/b; Histone H3/l; H3K9me; H3K9me1; H3K9

Background
Histone H3 lysine 9 monomethylation (H3K9me1) is a covalent post-translational modification occurring on the N-terminal tail of the core histone H3, a key component of the canonical nucleosome that organizes genomic DNA into chromatin. H3K9me1 is established by SET-domain-containing lysine methyltransferases, which can modify newly synthesized H3 during or immediately after translation to generate a pool of primed histones for chromatin incorporation. These monomethylated histones can serve as substrates for further methylation to H3K9me2 and H3K9me3, marks associated with heterochromatin formation, transcriptional repression, and the creation of silent chromatin domains. H3K9 methylation states modulate the recruitment of chromatin-associated factors, including reader proteins with aromatic-cage domains that discriminate between mono-, di-, and tri-methylated lysine. In certain plant species, a SAWADEE-like reader domain preferentially recognizes H3K9me1, indicating that this mark can act as a distinct docking site for effector complexes. H3K9 methylation can also antagonize local histone acetylation by restricting histone acetyltransferase access or activity, thereby reinforcing chromatin repression. Altered H3K9 methylation patterns, such as loss or redistribution of H3K9me1, have been linked to compromised heterochromatin maintenance, impaired transposon silencing, and gene regulation defects, contributing to developmental disorders and cancer. Positioned at the crossroads of histone turnover, hierarchical methylation, and reader recruitment, H3K9me1 serves as a key marker and functional probe for studying early heterochromatin assembly, RNA-directed DNA methylation, and the epigenetic regulation of genome stability.

Background

Histone H3 lysine 9 monomethylation (H3K9me1) is a covalent post-translational modification occurring on the N-terminal tail of the core histone H3, a key component of the canonical nucleosome that organizes genomic DNA into chromatin. H3K9me1 is established by SET-domain-containing lysine methyltransferases, which can modify newly synthesized H3 during or immediately after translation to generate a pool of primed histones for chromatin incorporation. These monomethylated histones can serve as substrates for further methylation to H3K9me2 and H3K9me3, marks associated with heterochromatin formation, transcriptional repression, and the creation of silent chromatin domains. H3K9 methylation states modulate the recruitment of chromatin-associated factors, including reader proteins with aromatic-cage domains that discriminate between mono-, di-, and tri-methylated lysine. In certain plant species, a SAWADEE-like reader domain preferentially recognizes H3K9me1, indicating that this mark can act as a distinct docking site for effector complexes. H3K9 methylation can also antagonize local histone acetylation by restricting histone acetyltransferase access or activity, thereby reinforcing chromatin repression. Altered H3K9 methylation patterns, such as loss or redistribution of H3K9me1, have been linked to compromised heterochromatin maintenance, impaired transposon silencing, and gene regulation defects, contributing to developmental disorders and cancer. Positioned at the crossroads of histone turnover, hierarchical methylation, and reader recruitment, H3K9me1 serves as a key marker and functional probe for studying early heterochromatin assembly, RNA-directed DNA methylation, and the epigenetic regulation of genome stability.

References
https://pubmed.ncbi.nlm.nih.gov/21243713/ https://pubmed.ncbi.nlm.nih.gov/21321607/

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%