Methyltransferase-like 3 (METTL3) and methyltransferase-like 14 (METTL14) form a stable heterodimer core complex that catalyzes N6-methyladenosine (m6A) RNA methylation in mammalian cells. m6A is an abundant internal modification in messenger RNA and long non-coding RNA.
It functions in multiple aspects of developmental regulation, cell cycle progression, cell fate, and the heat shock stress response by affecting aspects of RNA metabolism such as pre-mRNA processing, translation efficiency, transcript stability and miRNA biogenesis.
100 kDa (METTL3) and 84 kDa (METTL14). The METTL3 / METTL14 assay is performed inhouse using the methyltransferase-Glo TM assay kit.
Full-length recombinant human METTL3/METTL14 complex was expressed by baculovirus in Sf9 insect cells using an N-terminal GST tag. The purity of METTL3/METTL14 complex was determined to be approx. 90% by densitometry and molecular weight was established to be approx. 100 kDa (METTL3) and 84 kDa (METTL14). The METTL3 / METTL14 assay is performed inhouse using the methyltransferase-Glo TM assay kit.
The specific activity of METTL3/METTL14 was determined to be 750 pmol/min/mg as per activity assay protocol. Sample Kinase Activity Plot. Image Credit: SignalChem Biotech
For particular information on a given lot, users can see the related technical data sheet.
Sample Purity Data. Image Credit: SignalChem Biotech
For specific data on a provided lot, users can see the related technical data sheet.
Storage, stability, and shipping
The product should be stored at −70 °C. For optimal storage, the target can be aliquoted into smaller amounts following centrifugation and can be stored at the proposed temperature. For highly favorable performance, multiple freeze/thaw cycles and repeated handling should be avoided.
100 kDa (METTL3) and 84 kDa (METTL14)
- Liu J. et al: A METTL3–METTL14 complex mediates mammalian nuclear RNA N6-adenosine methylation. Nat. Chem. Biol. 2014; 10: 93–95
- Wang X. et al: Structural basis of N6-adenosine methylation by the METTL3–METTL14 complex. Nature 2016; 534:575-578
- Wang P. et al: Structural Basis for Cooperative Function of Mettl3 and Mettl14 Methyltransferases. Mol. Cell 2016; 63(2):306-317