100% Quality Guarantee
PhD-Level Technical Support
Key Features

Human DNMT2/TRDMT1 Recombinant Protein (GST Tag) (RPES2635)

SKU RPES2635
Product Type Recombinant Protein
Species Human
Application Area Epigenetic & Nuclear Proteins
€1,368

Request a formal quotation

A PDF quote with its own quote number, ready for your purchasing office to raise a PO against. Back within 4 working hours, from a PhD scientist — not an autoresponder.

  • PO-ready PDFQuote number, VAT, Incoterms
  • Volume pricing appliedDiscounts from 2 kits up
  • Valid 30 daysPrices held while you get sign-off
Anything we should know? optional

No account needed. We use your details only to prepare and send this quote. If it's urgent, say so in the box and we'll come back the same working day.

Global Shipping: 80+ Countries
White Glove Service: Available upon request
Batch Consistency: Contact Sales
Distributors: 60+ Countries

Description

system_update_altDatasheetsystem_update_altMSDS

Human DNMT2/TRDMT1 Recombinant Protein

DNMT2, also known as tRNA (cytosine-5-)-methyltransferase, DNA methyltransferase homolog HsaIIP, and TRDMT1, is a member of the DNA methyltransferase family of enzymes. DNMT2 enzymes have been widely conserved during evolution and contain all of the signature motifs of DNA (cytosine-5)-methyltransferases. It contains all 10 sequence motifs that are conserved among m(5)C MTases, including the consensus S:-adenosyl-L-methionine-binding motifs and the active site ProCys dipeptide, and its structure is very similar to prokaryotic DNA methyltransferases. DNMT2 has close homologs in plants, insects and Schizosaccharomyces pombe, but no related sequence can be found in the genomes of Saccharomyces cerevisiae or Caenorhabditis elegans. While the biological function of DNMT2 is not yet known, the strong binding to DNA suggests that DNMT2 may mark specific sequences in the genome by binding to DNA through the specific target-recognizing motif. However, the DNA methyltransferase activity of these proteins is comparatively weak and their biochemical and functional properties remain enigmatic. Recent evidence now shows that Dnmt2 has a novel tRNA methyltransferase activity, raising the possibility that the biological roles of these proteins might be broader than previously thought.

View AllClose

0 Reviews

0
Based on 0 reviews

No reviews yet. Be the first to share your experience!

View AllClose