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Immunohistochemical analysis of paraffin-embedded human breast carcinoma using Di-Methyl-Histone H3 (Lys4) (C64G9) Rabbit mAb #9725 in the presence of control peptide (left) or Di-Methyl Histone H3 (Lys4) Blocking Peptide (right).

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Product Description

This peptide is used to block Di-Methyl-Histone H3 (Lys4) (C64G9) Rabbit mAb #9725 reactivity in immunohistochemistry protocols.


Quality Control

The quality of the peptide was evaluated by reversed-phase HPLC and by mass spectrometry. The peptide blocks Di-Methyl Histone H3 (Lys4) (C64G9) Rabbit mAb #9725 by immunohistochemistry.

Product Usage Information

Use as a blocking reagent to evaluate the specificity of antibody reactivity in immunohistochemistry protocols. For immunohistochemistry, add twice the volume of peptide as volume of antibody used in 100 µl total volume. Incubate for a minimum of 30 minutes prior to adding the entire volume to the slide. Recommended antibody dilutions can be found on the relevant product data sheet.


Storage: Supplied in 20 mM potassium phosphate (pH 7.0), 50 mM NaCl, 0.1 mM EDTA, 1 mg/ml BSA and 5% glycerol. Store at –20°C.

The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (1). Histone methylation is a major determinant for the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development (2,3). Arginine methylation of histones H3 (Arg2, 17, 26) and H4 (Arg3) promotes transcriptional activation and is mediated by a family of protein arginine methyltransferases (PRMTs), including the co-activators PRMT1 and CARM1 (PRMT4) (4). In contrast, a more diverse set of histone lysine methyltransferases has been identified, all but one of which contain a conserved catalytic SET domain originally identified in the Drosophila Su(var)3-9, Enhancer of zeste, and Trithorax proteins. Lysine methylation occurs primarily on histones H3 (Lys4, 9, 27, 36, 79) and H4 (Lys20) and has been implicated in both transcriptional activation and silencing (4). Methylation of these lysine residues coordinates the recruitment of chromatin modifying enzymes containing methyl-lysine binding modules such as chromodomains (HP1, PRC1), PHD fingers (BPTF, ING2), tudor domains (53BP1), and WD-40 domains (WDR5) (5-8). The discovery of histone demethylases such as PADI4, LSD1, JMJD1, JMJD2, and JHDM1 has shown that methylation is a reversible epigenetic marker (9).


1.  Peterson, C.L. and Laniel, M.A. (2004) Curr Biol 14, R546-51.

2.  Kubicek, S. et al. (2006) Ernst Schering Res Found Workshop , 1-27.

3.  Lin, W. and Dent, S.Y. (2006) Curr Opin Genet Dev 16, 137-42.

4.  Lee, D.Y. et al. (2005) Endocr Rev 26, 147-70.

5.  Daniel, J.A. et al. (2005) Cell Cycle 4, 919-26.

6.  Shi, X. et al. (2006) Nature 442, 96-9.

7.  Wysocka, J. et al. (2006) Nature 442, 86-90.

8.  Wysocka, J. et al. (2005) Cell 121, 859-72.

9.  Trojer, P. and Reinberg, D. (2006) Cell 125, 213-7.


Entrez-Gene Id 8350
Swiss-Prot Acc. P68431


For Research Use Only. Not For Use In Diagnostic Procedures.
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