Pure human recombinant enzyme
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PRMT6 (human recombinant; baculovirus expressed)

Item No. 13866

Product Insert (PDF)
Technical Information
Synonyms
  • Histone Arginine N-methyltransferase PRMT6
  • HRMT1L6
  • Protein Arginine Methyltransferase 6
Purity
≥60%
Source
Recombinant N-terminal His-tagged protein expressed in Sf21 cells
Amino Acids
2-375 (full length)
MW
43.7 kDa
Formulation (Request formulation change)
50 mM Tris-HCl, pH 8.0, with 150 mM sodium chloride and 20% glycerol
UniProt Accession №
Q96LA8
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    50 µg

    $532

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    Product Description

    Protein arginine methyltransferases (PRMTs) are a family of enzymes with highly conserved catalytic domains that catalyze the transfer of a methyl group from S-adenosyl-L-methionine to a specific arginine residue in a target protein. PRMT6 is a nuclear type-1 PRMT, catalyzing the formation of ω-NG-monomethylarginine and asymmetric ω-NG,NG-dimethylarginine on both histone and non-histone targets.1,2,3 Histone H3 methylation of arginine 2 (H3R2) is a repressive transcriptional mark primarily catalyzed by PRMT6.4 H3R2 dimethylation antagonizes the binding of effector proteins sensitive to H3K4 methylation, such as the Mixed Lineage Leukemia complex methyltransferase.5 Non-histone targets of PRMT6 include the nuclear high-mobility group protein HMGA1a, a protein important in several processes relating to the maintenance of DNA integrity.3

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Frankel, A., Yadav, N., Lee, J., et al. The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. The Journal of Biological Chemisty 277(5), 3537-3543 (2002).

    2. Wolf, S.S. The protein arginine methyltransferase family: An update about function, new perspectives and the physiological role in humans. Cell. Mol. Life Sci. 66(13), 2109-2121 (2009).

    3. Miranda, T.B., Webb, K.J., Edberg, D.D., et al. Protein arginine methyltransferase 6 specifically methylates the nonhistone chromatin protein HMGA1a. Biochem. Biophys. Res. Commun. 336(3), 831-835 (2005).

    4. Iberg, A.N., Espejo, A., Cheng, D., et al. Arginine methylation of the histone H3 tail impedes effector binding. The Journal of Biological Chemisty 283(6), 3006-3010 (2008).

    5. Guccione, E., Bassi, C., Casadio, F., et al. Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive. Nature 449(7164), 933-937 (2007).