Render Target: STATIC
Render Timestamp: 2024-11-14T10:56:47.480Z
Commit: 3c1f305a63297e594ac8d7bb5424007d592d68be
XML generation date: 2024-10-28 20:01:13.464
Product last modified at: 2024-11-07T19:45:08.275Z
1% for the planet logo
PDP - Template Name: Antibody Sampler Kit
PDP - Template ID: *******4a3ef3a

Tri-Methyl Histone H3 Antibody Sampler Kit #9783

    Product Information

    Product Description

    Tri-Methyl Histone H3 Antibody Sampler Kit offers an economical means to evaluate the tri-methylation of Histone H3 on multiple residues. The kit contains enough primary antibody to perform two western blot experiments per primary.

    Specificity / Sensitivity

    Each modification-state Histone H3 antibody detects endogenous levels of Histone H3 only when tri-methylated on the indicated lysine residue. These antibodies do not cross-react with mono-methylated or di-methylated histone H3, or tri-methylated histone H4 at Lys20. Tri-Methyl-Histone H3 (Lys9) (D4W1U) Rabbit mAb detects endogenous levels of histone H3 when tri-methylated on Lys9. This antibody shows some cross-reactivity with histone H3 that is di-methylated on Lys9, but does not cross-react with non-methylated or mono-methylated histone H3 Lys9. This antibody does not detect tri-methyl histone H3 Lys9 when the adjacent Ser10 residue is phosphorylated during mitosis. In addition, this antibody does not cross-react with methylated histone H3 Lys4, Lys27, Lys36, or Lys79. Tri-Methyl-Histone H3 (Lys79) Antibody may show slight cross-reactivity toward histone H3 when di-methylated at Lys79, but does not cross-react with histone H3 tri-methylated at Lys4, 9, 27, or 36, or histone H4 at Lys20. Histone H3 (D1H2) XP® Rabbit mAb detects endogenous levels of total histone H3 protein. This antibody does not cross-react with other histones.

    Source / Purification

    Monoclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the amino terminus of histone H3 in which Lys4, Lys9, Lys27, and Lys36 are tri-methylated, respectively. Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding tri-methyl-Lys79. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.

    Background

    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).
    For Research Use Only. Not For Use In Diagnostic Procedures.
    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
    U.S. Patent No. 7,429,487, foreign equivalents, and child patents deriving therefrom.
    All other trademarks are the property of their respective owners. Visit our Trademark Information page.