5´ Deadenylase is capable of deadenylation from 5´-end of DNA and RNA, leaving the phosphate at 5´-end. It also cleaves AppppA into ATP and AMP.
- Isolated from a recombinant source
- Supplied with 10X reaction buffer
- Tested for the absence of DNases, RNases, and phosphatases
Avoiding RNase Contamination
Yeast 5´ Deadenylase is a member of the HIT (histidine triad) family proteins and specifically a member of the Hint branch. It is the yeast orthologue of aprataxin. Mutations in human aprataxin have been known to be involved in the neurological disorder known as ataxia oculomotor apraxia-1 (1). The human protein has been shown to resolve abortive ligation intermediates by removing the AMP at the 5´ end of DNA (AMP-DNA hydrolase activity) (2). It also repairs DNA damage at 3´ ends by removing 3´-phosphate and 3´-phosphoglycolate (3). Human aprataxin acts on small molecules as well, nucleotide polyphosphates such as diadenosine tetraphosphate (AppppA) as well as lysyl-AMP.
The 5´ Deadenylase is encoded by HNT3 gene of S. cerevisiae. NEB has shown this protein is capable of deadenylation from 5´ end of DNA and RNA, leaving the phosphate at 5´ end. It also cleaves AppppA into ATP and AMP. Its activity on lysyl-AMP is not detectable.
Product SourcePurified from an E. coli strain carrying a plasmid encoding 5´ Deadenylase from S. cerevisiae.
The following reagents are supplied with this product:
Store at (°C) Concentration NEBuffer™ 1 -20 10 X
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