|Application ||WB, E|
|Calculated MW||67769 Da|
|Other Names||Endonuclease 8-like 3, 322-, DNA glycosylase FPG2, DNA glycosylase/AP lyase Neil3, Endonuclease VIII-like 3, Nei-like protein 3, NEIL3|
|Target/Specificity||This NEIL3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 292-320 amino acids from the Central region of human NEIL3.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||NEIL3 Antibody(Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||DNA glycosylase which prefers single-stranded DNA (ssDNA), or partially ssDNA structures such as bubble and fork structures, to double-stranded DNA (dsDNA). In vitro, displays strong glycosylase activity towards the hydantoin lesions spiroiminodihydantoin (Sp) and guanidinohydantoin (Gh) in both ssDNA and dsDNA; also recognizes FapyA, FapyG, 5-OHU, 5-OHC, 5- OHMH, Tg and 8-oxoA lesions in ssDNA. No activity on 8-oxoG detected. Also shows weak DNA-(apurinic or apyrimidinic site) lyase activity. In vivo, appears to be the primary enzyme involved in removing Sp and Gh from ssDNA in neonatal tissues. Seems to be an important facilitator of cell proliferation in certain populations, for example neural stem/progenitor cells and tumor cells, suggesting a role in replication-associated DNA repair.|
|Tissue Location||Expressed in keratinocytes and embryonic fibroblasts (at protein level). Also detected in thymus, testis and fetal lung primary fibroblasts.|
Provided below are standard protocols that you may find useful for product applications.
NEIL3 belongs to a class of DNA glycosylases homologous to the bacterial Fpg/Nei family. These glycosylases initiate the first step in base excision repair by cleaving bases damaged by reactive oxygen species and introducing a DNA strand break via the associated lyase reaction (Bandaru et al., 2002 [PubMed 12509226]).
Krokeide, S.Z., et al. Protein Expr. Purif. 65(2):160-164(2009)
Takao, M., et al. Genes Cells 14(2):261-270(2009)
Dallosso, A.R., et al. Gut 57(9):1252-1255(2008)
Bethke, L., et al. J. Natl. Cancer Inst. 100(4):270-276(2008)
Newton-Cheh, C., et al. BMC Med. Genet. 8 SUPPL 1, S7 (2007) :