Mouse Neil3 ELISA Kit (V2LY-0626-LY2332)

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Tested Data
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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Sensitivity
0.0099 ng/mL
Detection Range
0.02-4.5 ng/mL
Sample Type
Serum, Plasma, cell culture supernates
Specificity
Mouse
Assay Type
Sandwich
Reactivity
Mouse
Assay Time
1.5 h
Molecule Mass
67.4 kDa
Components
  • Pre-coated ELISA plate: 12 wells * 8 detachable strips
  • Standard solution: 0.5ml x1
  • Standard diluent: 3ml x1
  • Streptavidin-HRP: 6ml x1
  • Stop solution: 6ml x1
  • Substrate solution A: 6ml x1
  • Substrate solution B: 6ml x1
  • Wash buffer concentrate (25x): 20ml x1
  • Biotinylated antibody: 1ml x1

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at 2-8°C
More Infomation

Target

Full Name
nei like 3 (E. coli)
Function
DNA glycosylase which prefers single-stranded DNA (ssDNA), or partially ssDNA structures such as bubble and fork structures, to double-stranded DNA (dsDNA) (PubMed:12433996, PubMed:19170771, PubMed:22569481, PubMed:23755964).

Mediates interstrand cross-link repair in response to replication stress: acts by mediating DNA glycosylase activity, cleaving one of the two N-glycosyl bonds comprising the interstrand cross-link, which avoids the formation of a double-strand break but generates an abasic site that is bypassed by translesion synthesis polymerases (By similarity).

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 (PubMed:12433996, PubMed:19170771, PubMed:22569481, PubMed:23755964).

No activity on 8-oxoG detected (PubMed:12433996, PubMed:19170771, PubMed:22569481, PubMed:23755964).

Also shows weak DNA-(apurinic or apyrimidinic site) lyase activity (PubMed:12433996, PubMed:19170771, PubMed:22569481, PubMed:23755964).

In vivo, appears to be the primary enzyme involved in removing Sp and Gh from ssDNA in neonatal tissues (PubMed:12433996, PubMed:19170771, PubMed:22569481, PubMed:23755964).
Biological Process
Base-excision repair Source: HGNC
Base-excision repair, AP site formation Source: Reactome
Depurination Source: Reactome
Interstrand cross-link repair Source: UniProtKB
Cellular Location
Nucleus
Other locations
Chromosome
Note: Recruited to replication stress sites via interaction with ubiquitinated CMG helicase.

Li, N., Xu, Y., Chen, H., Chen, L., Zhang, Y., Yu, T., ... & Wang, J. (2022). NEIL3 contributes to the Fanconi anemia/BRCA pathway by promoting the downstream double-strand break repair step. Cell Reports, 41(6).

Wang, Q., Li, Z., Yang, J., Peng, S., Zhou, Q., Yao, K., ... & Huang, H. (2022). Loss of NEIL3 activates radiotherapy resistance in the progression of prostate cancer. Cancer biology & medicine, 19(8), 1193-1210.

Lai, H. H., Hung, L. Y., Yen, C. J., Hung, H. C., Chen, R. Y., Ku, Y. C., ... & Huang, W. (2022). NEIL3 promotes hepatoma epithelial–mesenchymal transition by activating the BRAF/MEK/ERK/TWIST signaling pathway. The Journal of Pathology, 258(4), 339-352.

Wang, W., Yin, Q., Guo, S., & Wang, J. (2021). NEIL3 contributes toward the carcinogenesis of liver cancer and regulates PI3K/Akt/mTOR signaling. Experimental and Therapeutic Medicine, 22(4), 1-11.

Zhao, C., Liu, J., Zhou, H., Qian, X., Sun, H., Chen, X., ... & Zhang, J. (2021). NEIL3 may act as a potential prognostic biomarker for lung adenocarcinoma. Cancer cell international, 21, 1-16.

Li, N., Wang, J., Wallace, S. S., Chen, J., Zhou, J., & D’Andrea, A. D. (2020). Cooperation of the NEIL3 and Fanconi anemia/BRCA pathways in interstrand crosslink repair. Nucleic Acids Research, 48(6), 3014-3028.

Nejad, M. I., Housh, K., Rodriguez, A. A., Haldar, T., Kathe, S., Wallace, S. S., ... & Gates, K. S. (2020). Unhooking of an interstrand cross-link at DNA fork structures by the DNA glycosylase NEIL3. DNA repair, 86, 102752.

Tran, O. T., Tadesse, S., Chu, C., & Kidane, D. (2020). Overexpression of NEIL3 associated with altered genome and poor survival in selected types of human cancer. Tumor Biology, 42(5), 1010428320918404.

Fleming, A. M., Zhu, J., Howpay Manage, S. A., & Burrows, C. J. (2019). Human NEIL3 gene expression regulated by epigenetic-like oxidative DNA modification. Journal of the American Chemical Society, 141(28), 11036-11049.

Albelazi, M. S., Martin, P. R., Mohammed, S., Mutti, L., Parsons, J. L., & Elder, R. H. (2019). The biochemical role of the human NEIL1 and NEIL3 DNA glycosylases on model DNA replication forks. Genes, 10(4), 315.

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For research use only. Not intended for any clinical use.

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