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Selectively cleaves DNA at the second phosphodiester bond 3' to hypoxanthine- and uracil-containing nucleotides. Additionally we are shipping Endonuclease V Proteins (3) and many more products for this protein.
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Mouse Endonuclease V shares substrate preferences with human EndoV by catalyzing cleavage at inosines in RNA and being inert towards inosines in DNA.
hEndoV is redistributed to stress granules as a strategy to create a local environment low in ATP to permit hEndoV activity.
Inosine-specific ribonuclease activity of natural variants of human endonuclease V
ENDOV was significantly associated with schizophrenia.
Human EndoV appears inactive on DNA, but has been shown to incise various RNA substrates containing inosine. [review]
This previously unknown RNA incision activity may suggest a role for endonuclease V in normal RNA metabolism.
hEndoV controls the fate of inosine-containing RNA in humans.
ENDOV is localized in the cytoplasm and nucleoli of human cells.
Selectively cleaves DNA at the second phosphodiester bond 3' to hypoxanthine- and uracil-containing nucleotides. Shows higher activity towards single-stranded than double-stranded DNA and towards hypoxanthine than uracil.
novel endonuclease V protein
, putative endonuclease FLJ39025 homolog