Anti- Histone H3c1 Antibody

Control
Recombinant Histone H3

Evaluated by Western Blot in recombinant Histone H3.

Western Blot Analysis: 0.5 µg/mL of this antibody detected unmethylated Histone H3 (Lys9) in 10 µg of recombinant Histone H3.

Research Category
Epigenetics & Nuclear Function

Research Sub Category
Histones

Use Anti-unmethylated-Histone H3 (Lys9) Antibody, clone 9B1-2G6 (Mouse Monoclonal Antibody) demonstrated to detect unmethylated-Histone H3 (Lys9) also known as Histone H3.1.

Western Blot Analysis: 0.5 µg/mL from a representative lot detected unmethylated Histone H3 (Lys9) in 10 µg of HeLa acid extract.

Dot Blot Analysis: Absurance Histone H3 Antibody Specificity Array (Cat. No. 16-667) and Absurance Histone H2A, H2B, H4 Antibody Specificity Array (Cat. No. 16-665), which contain histone peptides with various modifications were probed with Cat. No MABE263-S, unmethylated-Histone H3 (Lys9), clone 9B1-2G6 at 0.5 µg/mL (1:2,000) dilution. Proteins were visualized using a Donkey anti-rabbit IgG conjugated to HRP and a chemiluminescence detection system.

Dot Blot (Specificity) Analysis: A representative lot detected non-methylated Histone H3 (Lys9) in Dot Blot. This antibody detects non-methylated Histone H3 (Lys9) when Ser10 is phosphorylated. It also detects mono-/di-methyl-Histone H3(Lys4), and Acetyl-Histone H3 (Lys14). (Prof. E. Ogris, Department of Medical Biochemistry, Medical University of Vienna).

This antibody recognizes Histone H3 unmethylated at Lys9. This antibody does not cross react with methyl-Histone (Lys29). This antibody detects unmethylated Histone H3 (Lys9) when Ser10 is phosphorylated. It also detects mono-/di-methyl-Histone H3 (Lys4), and Acetyl-Histone H3 (Lys14). (Prof. E. Ogris, Department of Medical Biochemistry, Medical University of Vienna).

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Histones are nuclear proteins that form octameric structures which bind DNA to form units of chromatin called nucleosomes. The family of histones—H2A, H2B, H3, and H4—are key players in gene regulation. They undergo a number of post-translational modifications (PTM) in response to various stimuli, including phosphorylation on serine and threonine residues and methylation on lysine residues. PTMs produce configural changes in histone proteins that may induce nucleosome remodeling and expose or hide DNA sequences from transcriptional complexes. Methylation occurs on histone H3 at lysine 4, 9, 27, 36, and 79 residues. Previous studies have reported that methylation of H3 lysine 9 provides a binding site for heterochromatin adaptor proteins (HP1) which are involved in the formation of heterochromatin and gene repression. Conversely,deacetylation of histone H3 lysine 9 is associated with gene-activating events. Often, it is the pattern of different modifications on several histone residues that alter chromatin, rather than modification of single residues.

~15 kDa observed

Epitope: unmethylated Lys9

KLH-conjugated linear peptide corresponding to human unmethylated Histone H3 (Lys9).

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Format: Purified

Protein G Purified

Purified mouse monoclonal IgG1κ supernatant in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.