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RNase 4 is a single-stranded RNA endonuclease that cleaves 3´ of uridine in uridine-purine sequences (cut sites: U/A and U/G). RNase 4 allows more targeted digestion of substrate RNA compared to single-nucleotide specific RNases like T1 (cut site: after G), RNase U2 (cut sites: after A and G), or bovine pancreatic RNase A (cut sites: after C and U). RNase 4 endonuclease activity tolerates uridine base modifications such as pseudo-, N1-methyl-pseudo-, dihydro-, and 5-methoxy-uridine species (Ψ, m1Ψ, D, and mo5U). Due to the chemical mechanism of RNase 4 endonucleolytic cleavage, product oligonucleotides contain heterogenous 3´ ends, where most species contain a linear 3´-phosphate or cyclic 2´,3´-phosphate.
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| Description |
RNase 4 is a single-stranded RNA endonuclease that cleaves 3´ of uridine in uridine-purine sequences (cut sites: U/A and U/G). RNase 4 allows more targeted digestion of substrate RNA compared to single-nucleotide specific RNases like T1 (cut site: after G), RNase U2 (cut sites: after A and G), or bovine pancreatic RNase A (cut sites: after C and U). RNase 4 endonuclease activity tolerates uridine base modifications such as pseudo-, N1-methyl-pseudo-, dihydro-, and 5-methoxy-uridine species (Ψ, m1Ψ, D, and mo5U). Due to the chemical mechanism of RNase 4 endonucleolytic cleavage, product oligonucleotides contain heterogenous 3´ ends, where most species contain a linear 3´-phosphate or cyclic 2´,3´-phosphate. |