Active • Host: E. coli • AA: 190-352 • Tag: N-terminal His • MW: 21.2 kDa
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SET8 (human recombinant)

Item No. 10319

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • KMT5a
  • PR-Set7
  • SETD8
  • SET domain-containing (lysine methyltransferase) 8
Purity
≥90% estimated by SDS-PAGE
Source
Active recombinant N-terminal hexahistidine-tagged protein purified from E. coli
Amino Acids
190-352
MW
21.1 kDa
Formulation (Request formulation change)
50 mM sodium phosphate, pH 7.2, with 100 mM sodium chloride and 20% glycerol
UniProt Accession №
Q9NQR1
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $442

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    Product Description

    Methylation of lysine can promote transcriptional activation or repression and is critical in regulating histone function. Lysine residues can be mono-, di-, or tri-methylated.1 SET8 selectively mono-methylates histone H4 at lysine 20, an event proven to have an important role in chromatin structure and transcriptional activation.2,3 SET8 is also a novel regulator of p53, mono-methylating lysine 382 of the tumor suppressor.4 SET8’s ability to suppress p53 transcriptional activity implies that it may play a significant role in tumorigenesis.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Bhaumik, S.R., Smith, E., and Shilatifard, A. Covalent modifications of histones during development and disease pathogenesis. Nat. Struct. Mol. Biol. 14(11), 1008-1016 (2007).

    2. Couture, J.F., Collazo, E., Brunzelle, J.S., et al. Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase. Genes Dev. 19(12), 1455-1465 (2005).

    3. Yin, Y., Liu, C., Tsai, S.N., et al. SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone H4 and mono-methylates lysine 20. The Journal of Biological Chemisty 280(34), 30025-30031 (2005).

    4. Shi, X., Kachirskaia, I., Yamaguchi, H., et al. Modulation of p53 function by SET8-mediated methylation at lysine 382. Mol. Cell 27(4), 636-646 (2007).