|Other Names||Endonuclease 8-like 2, 322-, DNA glycosylase/AP lyase Neil2, DNA-(apurinic or apyrimidinic site) lyase Neil2, Endonuclease VIII-like 2, Nei homolog 2, NEH2, Nei-like protein 2, NEIL2|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Has DNA glycosylase activity towards 5-hydroxyuracil and other oxidized derivatives of cytosine with a preference for mismatched double-stranded DNA (DNA bubbles). Has low or no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine, hypoxanthine and 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.|
|Tissue Location||Detected in testis, skeletal muscle, heart, brain, placenta, lung, pancreas, kidney and liver|
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Provided below are standard protocols that you may find useful for product applications.
NEIL2 belongs to a class of DNA glycosylases homologous tothe bacterial Fpg/Nei family. These glycosylases initiate the firststep in base excision repair by cleaving bases damaged by reactiveoxygen species and introducing a DNA strand break via theassociated lyase reaction (Bandaru et al., 2002 [PubMed12509226])
Briggs, F.B., et al. Am. J. Epidemiol. 172(2):217-224(2010)Monsees, G.M., et al. Breast Cancer Res. Treat. (2010) In press :Grin, I.R., et al. Biochem. Biophys. Res. Commun. 394(1):100-105(2010)Kinslow, C.J., et al. Genes Chromosomes Cancer 47(11):923-932(2008)Zhai, X., et al. Clin. Cancer Res. 14(13):4345-4352(2008)
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