For immunochemical detection of histone H3K36Me2
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Histone H3K36Me2 Monoclonal Antibody (RM141)

Item No. 32133

Technical Information
Synonyms
  • Dimethylated Histone H3 Lysine 36
Immunogen
Peptide corresponding to H3K36Me2
Clone Designation
RM141
100 µg of protein A-affinity purified monoclonal antibody
Storage Buffer
PBS with 50% glycerol, 1% BSA, and 0.09% sodium azide
Host
Rabbit
Isotype
IgG
Applications
ELISA, multiplex-based assays, WB
Cross Reactivity
(+) H3K36Me2(-) Unmodified H3K36(-) H3K36Me1(-) H3K36Me3(-) H3K4Me1(-) H3K4Me2(-) H3K4Me3(-) H3K9Me1(-) H3K9Me2(-) H3K9Me3(-) H3K14Me2(-) H3K18Me1(-) H3K18Me2(-) H3K23Me1(-) H3K23Me2(-) H3K27Me1(-) H3K27Me2(-) H3K27Me3(-) H3K56Me1(-) H3K79Me1(-) H3K79Me2(-) H3K79Me3
Species Reactivity
(+) Vertebrates
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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Certificates of Analysis & Batch Specific Data

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    Product Description

    Histone H3 is a nuclear protein and a component of the nucleosome core, a basic unit of chromatin, that is essential for organizing genomic DNA in eukaryotic nuclei.1 It is a globular protein that contains an unstructured N-terminal tail that extends outside of the nucleosome core and is subject to various post-translational modifications (PTMs), including methylation, phosphorylation, acetylation, and citrullination.1,2 Dimethylation of H3K36 is catalyzed by SET domain-containing histone methyltransferases including SET2, HYPB, NSD1, and ASH1L, and mutation of these methyltransferases is associated with various diseases, including multiple myeloma and Sotos syndrome.3,4,5 H3K36Me2 is enriched at the coding regions of genes and correlates with the initiation, but not maintenance, of active transcription, heterochromatin maintenance, and DNA break repair.4,6,7 Cayman's Histone H3K36Me2 Monoclonal Antibody (RM141) can be used for ELISA, multiplex-based assays, and Western blot (WB) applications.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Hyun, K., Jeon, J., Park, K., et al. Writing, erasing and reading histone lysine methylations. Exp. Mol. Med. 49(4), e324 (2017).

    2. Sharda, A., Amnekar, R.V., Natu, A., et al. Histone posttranslational modifications: Potential role in diagnosis, prognosis, and therapeutics of cancer. Prognostic Epigenetics 15, 351-373 (2019).

    3. Li, J., Ahn, J.H., and Wang, G.G. Understanding histone H3 lysine 36 methylation and its deregulation in disease. Cell Mol. Life Sci. 76(15), 2899-2916 (2019).

    4. Rao, B., Shibata, Y., Strahl, B.D., et al. Dimethylation of histone H3 at lysine 36 demarcates regulatory and nonregulatory chromatin genome-wide. Mol. Cell. Biol. 25(21), 9447-9459 (2005).

    5. Sun, X.J., Wei, J., Wu, X.Y., et al. Identification and characterization of a novel human histone H3 lysine 36-specific methyltransferase. The Journal of Biological Chemisty 280(42), 35261-35271 (2005).

    6. Li, B., Jackson, J., Simon, M.D., et al. Histone H3 lysine 36 dimethylation (H3K36me2) is sufficient to recruit the Rpd3s histone deacetylase complex and to repress spurious transcription. The Journal of Biological Chemisty 284(12), 7970-7976 (2009).

    7. Avdic, V., Zhang, P., Lanouette, S., et al. Structural and biochemical insights into MLL1 core complex assembly. Structure 19(1), 101-108 (2011).