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AB123204

Recombinant Human NEIL1 protein (His tag N-Terminus)

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Recombinant Human NEIL1 protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 390 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

Endonuclease 8-like 1, DNA glycosylase/AP lyase Neil1, DNA-(apurinic or apyrimidinic site) lyase Neil1, Endonuclease VIII-like 1, FPG1, Nei homolog 1, Nei-like protein 1, NEH1, NEIL1

1 Images
SDS-PAGE - Recombinant Human NEIL1 protein (His tag N-Terminus) (AB123204)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human NEIL1 protein (His tag N-Terminus) (AB123204)

15% SDS-PAGE analysis of ab123204 (3ug)

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

Q96FI4

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

EC=3.2.2.
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMPEGPELHLASQFVNEACRALVFGGCVEKSSVSRNPEVPFESSAYRISASARGKELRLILSPLPGAQPQQEPLALVFRFGMSGSFQLVPREELPRHAHLRFYTAPPGPRLALCFVDIRRFGRWDLGGKWQPGRGPCVLQEYQQFRENVLRNLADKAFDRPICEALLDQRFFNGIGNYLRAEILYRLKIPPFEKARSVLEALQQHRPSPELTLSQKIRTKLQNPDLLELCHSVPKEVVQLGGKGYGSESGEEDFAAFRAWLRCYGMPGMSSLQDRHGRTIWFQGDPGPLAPKGRKSRKKKSKATQLSPEDRVEDALPPSKAPSRTRRAKRDLPKRTATQRPEGTSLQQDPEAPTVPKKGRRKGRQAASGHCRPRKVKADIPSLEPEGTSAS","proteinLength":"Full Length","predictedMolecularWeight":"45.8 kDa","actualMolecularWeight":null,"aminoAcidEnd":390,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q96FI4","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

NEIL1 also known as Nei endonuclease VIII-like 1 functions as a DNA glycosylase involved in base excision repair. This protein has a molecular mass of approximately 44 kDa. NEIL1 operates on oxidatively damaged bases in DNA removing lesions from DNA to maintain genome integrity. Expression of NEIL1 occurs in various tissues with higher levels often found in the liver and other metabolically active organs.
Biological function summary

NEIL1 plays an important role in the DNA damage repair process ensuring stability and integrity of the genome. It is particularly active in removing oxidative damage to bases functioning as part of the base excision repair pathway. NEIL1 works in coordination with other proteins such as DNA polymerase and ligase to repair DNA. It does not exist alone but forms complexes with these and other DNA repair proteins to carry out its role efficiently.

Pathways

NEIL1 acts within the base excision repair and nucleotide excision repair pathways. These pathways are vital for correcting DNA damage caused by oxidative stress and other environmental factors. In these pathways NEIL1 interacts with other repair enzymes including DNA polymerase beta to ensure proper coordination during the repair process. The interaction helps streamline the replacement and sealing of damaged DNA segments.

Alterations in NEIL1 function associate with various conditions specifically cancer and neurodegenerative diseases. Mutations or deficiencies in NEIL1 can lead to improper repair of DNA contributing to carcinogenesis. Moreover research indicates NEIL1 may interact with other proteins like p53 a known tumor suppressor linking its role in tumor development and suppression. In neurodegenerative diseases faulty DNA repair mechanisms involving NEIL1 contribute to neuronal damage and disease progression.
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Specifications

Form

Liquid

Additional notes

ab123204 is purified using conventional chromatography.

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General info

Function

Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as a DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 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. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U : C and T : C mismatches. Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC.

Sequence similarities

Belongs to the FPG family.

Subcellular localisation

Cytoskeleton

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Product protocols

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Target data

Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as a DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 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. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U : C and T : C mismatches. Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC.
See full target information Endonuclease 8-like 1
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