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Render Timestamp: 2024-12-26T11:06:05.670Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-11-18 16:03:10.495
Product last modified at: 2024-11-19T09:00:34.519Z
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PDP - Template Name: InTraSeq Conjugate
PDP - Template ID: *******e148868
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Tri-Methyl-Histone H3 (Lys27) (C36B11) Rabbit mAb (InTraSeq 3' Conjugate 3017) #53207

Filter:
  • SCA

    Supporting Data

    REACTIVITY H M
    SENSITIVITY Endogenous
    MW (kDa)
    Source/Isotype Rabbit IgG
    Application Key:
    • SCA-Single Cell Analysis 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 

    Product Information

    Storage

    Supplied in PBS (pH 7.2), 2 mM EDTA, 0.05% Triton X-100, 2 mg/mL BSA, and 50% glycerol. Store at -20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Tri-Methyl-Histone H3 (Lys27) (C36B11) Rabbit mAb (InTraSeq™ 3' Conjugate 3017) detects endogenous levels of histone H3 only when tri-methylated on Lys27. The antibody does not cross-react with non-methylated, mono-methylated or di-methylated Lys27. In addition, the antibody does not cross-react with mono-methylated, di-methylated or tri-methylated histone H3 at Lys4, Lys9, Lys36 or Histone H4 at Lys20.

    Species Reactivity:

    Human, Mouse

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to the amino terminus of histone H3 in which Lys27 is tri-methylated.

    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.
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    10x Genomics, 10x, Feature Barcode, and Chromium are the trademarks or registered trademarks of 10x Genomics, Inc.
    InTraSeq is a trademark of Cell Signaling Technology, Inc.
    Subject to patents licensed from 10x Genomics, Inc. for use with single-cell (i.e., Chromium) 10x products.
    U.S. Patent No. 7,429,487, foreign equivalents, and child patents deriving therefrom.
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