• Product name

    Recombinant human KMT5A / SETD8 / Pr-SET7 protein
    See all KMT5A / SETD8 / Pr-SET7 proteins and peptides
  • Biological activity

    50 µl reaction mix (50 mM Tris, pH 8.8, 1 mM EDTA, 1 mM DTT, 40 µM S-adenosylhomocysteine, and 0-6 µg ab196432) is added to the wells coated with the substrate. Incubate for 2 hr. Add antibody against methylated residue of histone H4, incubate 1 hr. Then, add secondary HRP-labeled antibody and incubate 30 min. Finally, add HRP chemiluminsecent substrates and read luminescence.

  • Purity

    >= 84 % SDS-PAGE.

  • Expression system

    Escherichia coli
  • Accession

  • Protein length

    Protein fragment
  • Animal free

  • Nature

    • Species

    • Sequence

    • Predicted molecular weight

      44 kDa including tags
    • Amino acids

      195 to 352
    • Tags

      GST tag N-Terminus
    • Additional sequence information

      Genbank accession number: NM_020382

Associated products


Our Abpromise guarantee covers the use of ab196432 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications


    Functional Studies

  • Form

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on Dry Ice. Store at -80°C. Avoid freeze / thaw cycle.

    pH: 8.0
    Constituents: 0.63% Tris HCl, 0.64% Sodium chloride, 0.02% Potassium chloride, 0.05% DTT, 20% Glycerol, 0.49% Glutathione

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

General Info

  • Alternative names

    • H4 K20 HMTase
    • H4 K20 specific histone methyltransferase
    • H4-K20-HMTase SETD8
    • Histone H4 K20 methyltransferase
    • Histone lysine N methyltransferase H4 lysine 20 specific
    • Histone-lysine N-methyltransferase SETD8
    • Lysine N-methyltransferase 5A
    • N-lysine methyltransferase SETD8
    • Pr SET 7
    • Pr SET7
    • PR-Set7
    • PR/SET domain containing protein 07
    • PR/SET domain containing protein 8
    • PR/SET domain-containing protein 07
    • PR/SET07
    • PrSET7
    • SET 07
    • SET 8
    • SET domain containing (lysine methyltransferase) 8
    • SET domain containing 8
    • SET domain containing lysine methyltransferase 8
    • SET domain containing protein 8
    • SET domain-containing protein 8
    • SET07
    • SET8
    • SETD 8
    • setd8
    see all
  • Function

    Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes.
  • Sequence similarities

    Belongs to the histone-lysine methyltransferase family. PR/SET subfamily.
    Contains 1 SET domain.
  • Developmental stage

    Not detected during G1 phase. First detected during S through G2 phases, and peaks during mitosis (at protein level).
  • Domain

    Although the SET domain contains the active site of enzymatic activity, both sequences upstream and downstream of the SET domain are required for methyltransferase activity.
  • Cellular localization

    Nucleus. Chromosome. Specifically localizes to mitotic chromosomes. Associates with silent chromatin on euchromatic arms. Not associated with constitutive heterochromatin.
  • Information by UniProt


  • SDS-PAGE analysis of 7.5 μg of ab196432 on a 4-20% SDS-PAGE gel stained with Coomassie.

  • Specific activity of ab196432.


ab196432 has not yet been referenced specifically in any publications.

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