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Mouse Anti-NEIL3 Recombinant Antibody (CBWJN-1315) (CBMAB-N1911-WJ)

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Datasheet
SDS
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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal
Mouse
Clone
CBWJN-1315
Application
WB
Specificity
Human
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Buffer
PBS, pH 7.4, 1% BSA
Preservative
0.05% sodium azide
Concentration
1 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
More Infomation

Target

Full Name
nei like 3 (E. coli)
Introduction
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]).[supplied by OMIM, Mar 2008]
Entrez Gene ID
55247
UniProt ID
Q8TAT5
Alternative Names
Nei Like DNA Glycosylase 3; Zinc Finger, GRF-Type Containing 3; DNA Glycosylase/AP Lyase Neil3; Endonuclease VIII-Like 3; DNA Glycosylase FPG2; Nei-Like Protein 3; Nei Endonuclease VIII-Like 3 (E. Coli); Nei Endonuclease VIII-Like 3; DNA Glycosylase HFPG2; Endonuclease 8-Like 3;
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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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Isotype control

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

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