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Mouse Anti-NEIL2 Recombinant Antibody (CBWJN-0312) (CBMAB-N0240-WJ)

This product is a Mouse antibody that recognizes NEIL2. The antibody CBWJN-0312 can be used for immunoassay techniques such as: Dot, WB.
See all NEIL2 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBWJN-0312
Antibody Isotype
IgG1
Application
Dot, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG1
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 7.2, 1% BSA
Preservative
0.05% sodium azide
Concentration
0.1 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.

Target

Full Name
Nei Like DNA Glycosylase 2
Introduction
This gene encodes a member of the Fpg/Nei family of DNA glycosylases. These glycosylases initiate the first step in base excision repair by cleaving oxidatively damaged bases and introducing a DNA strand break via their abasic site lyase activity. This enzyme is primarily associated with DNA repair during transcription and acts prefentially on cytosine-derived lesions, particularly 5-hydroxyuracil and 5-hydroxycytosine. It contains an N-terminal catalytic domain, a hinge region, and a C-terminal DNA-binding domain with helix-two-turn-helix and zinc finger motifs. This enzyme interacts with the X-ray cross complementing factor 1 scaffold protein as part of a multi-protein DNA repair complex. A pseudogene of this gene has been identified. [provided by RefSeq, Mar 2017]
Entrez Gene ID
252969
UniProt ID
Q969S2
Alternative Names
Nei Like DNA Glycosylase 2; DNA-(Apurinic Or Apyrimidinic Site) Lyase Neil2; DNA Glycosylase/AP Lyase Neil2; Nei-Like Protein 2; Nei Homolog 2; NEH2; Nei Endonuclease VIII-Like 2 (E. Coli); Nei Endonuclease VIII-Like 2;
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.
Biological Process
Base-excision repair Source: GO_Central
Depyrimidination Source: Reactome
Cellular Location
Nucleus

Tapryal, N., Chakraborty, A., Saha, K., Islam, A., Pan, L., Hosoki, K., ... & Hazra, T. K. (2023). The DNA glycosylase NEIL2 is protective during SARS-CoV-2 infection. Nature Communications, 14(1), 8169.

Zhdanova, P. V., Ishchenko, A. A., Chernonosov, A. A., Zharkov, D. O., & Koval, V. V. (2022). Dynamics and conformational changes in human NEIL2 DNA glycosylase analyzed by hydrogen/deuterium exchange mass spectrometry. Journal of Molecular Biology, 434(2), 167334.

Hanna, B. M., Michel, M., Helleday, T., & Mortusewicz, O. (2021). NEIL1 and NEIL2 Are Recruited as Potential Backup for OGG1 upon OGG1 Depletion or Inhibition by TH5487. International Journal of Molecular Sciences, 22(9), 4542.

Sarker, A. H., Cooper, P. K., & Hazra, T. K. (2021). DNA glycosylase NEIL2 functions in multiple cellular processes. Progress in biophysics and molecular biology, 164, 72-80.

Eckenroth, B. E., Cao, V. B., Averill, A. M., Dragon, J. A., & Doublié, S. (2021). Unique structural features of mammalian NEIL2 DNA glycosylase prime its activity for diverse DNA substrates and environments. Structure, 29(1), 29-42.

Tapryal, N., Shahabi, S., Chakraborty, A., Hosoki, K., Wakamiya, M., Sarkar, G., ... & Hazra, T. K. (2021). Intrapulmonary administration of purified NEIL2 abrogates NF-κB–mediated inflammation. Journal of Biological Chemistry, 296.

Cumova, A., Vymetalkova, V., Opattova, A., Bouskova, V., Pardini, B., Kopeckova, K., ... & Vodicka, P. (2021). Genetic variations in 3′ UTRs of SMUG1 and NEIL2 genes modulate breast cancer risk, survival and therapy response. Mutagenesis, 36(4), 269-279.

Sayed, I. M., Sahan, A. Z., Venkova, T., Chakraborty, A., Mukhopadhyay, D., Bimczok, D., ... & Das, S. (2020). Helicobacter pylori infection downregulates the DNA glycosylase NEIL2, resulting in increased genome damage and inflammation in gastric epithelial cells. Journal of Biological Chemistry, 295(32), 11082-11098.

Sayed, I. M., Chakraborty, A., El-Hafeez, A., Ali, A., Sharma, A., Sahan, A. Z., ... & Das, S. (2020). The DNA glycosylase NEIL2 suppresses fusobacterium-infection-induced inflammation and DNA damage in colonic epithelial cells. Cells, 9(9), 1980.

Han, D., Schomacher, L., Schüle, K. M., Mallick, M., Musheev, M. U., Karaulanov, E., ... & Niehrs, C. (2019). NEIL1 and NEIL2 DNA glycosylases protect neural crest development against mitochondrial oxidative stress. elife, 8, e49044.

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

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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