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AB113607

Recombinant Human NTH1 protein

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Recombinant Human NTH1 protein is a Human Full Length protein, in the 1 to 312 aa range, expressed in Escherichia coli, with >80%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

NTH1, OCTS3, NTHL1, Endonuclease III-like protein 1, hNTH1, Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase, DNA glycosylase/AP lyase

1 Images
SDS-PAGE - Recombinant Human NTH1 protein (AB113607)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human NTH1 protein (AB113607)

15% SDS-PAGE analysis of ab113607 (3μg)

Key facts

Purity

>80% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

P78549

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 40% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

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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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMCSPQESGMTALSARMLTRSRSLGPGAGPRGCREEPGPLRRREAAAEARKSHSPVKRPRKAQRLRVAYEGSDSEKGEGAEPLKVPVWEPQDWQQQLVNIRAMRNKKDAPVDHLGTEHCYDSSAPPKVRRYQVLLSLMLSSQTKDQVTAGAMQRLRARGLTVDSILQTDDATLGKLIYPVGFWRSKVKYIKQTSAILQQHYGGDIPASVAELVALPGVGPKMAHLAMAVAWGTVSGIAVDTHVHRIANRLRWTKKATKSPEETRAALEEWLPRELWHEINGLLVGFGQQTCLPVHPRCHACLNQALCPAAQGL","proteinLength":"Full Length","predictedMolecularWeight":"36.6 kDa","actualMolecularWeight":null,"aminoAcidEnd":312,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P78549","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.

The NTH1 protein also known as endonuclease III-like protein 1 functions as a DNA glycosylase involved in base excision repair. It plays a role in the repair of oxidative DNA damage. NTH1 has a molecular mass of approximately 33 kDa. This protein is located in various tissues throughout the human body but it shows higher expression in the testes heart and skeletal muscle. These expression patterns suggest its significance in oxidative stress response across different body systems.
Biological function summary

NTH1 removes oxidized pyrimidines from damaged DNA as part of its role in cellular repair mechanisms. As a component of the base excision repair pathway it tackles oxidative lesions to prevent mutation accumulation. It does not act as a complex with other proteins but operates after being recruited to relevant DNA sites requiring repair. This essential function keeps genomic integrity intact and allows for regular cellular processes.

Pathways

NTH1 plays an important role within the base excision repair and DNA damage response pathways. It cooperates with proteins such as APE1 which prepares the site for subsequent repair steps ensuring proper DNA maintenance. NTH1’s involvement in base excision repair specifically addresses small-scale oxidative damage highlighting its role in safeguarding genetic information. These pathways are fundamental for normal cell function and response to environmental stressors.

NTH1 has links to conditions involving accumulated DNA damage such as cancer and neurodegenerative diseases. DNA repair deficiency due to NTH1 malfunction can contribute to the onset of such diseases. The protein interacts with partners like OGG1 which also plays a role in oxidative DNA lesion recognition and repair to manage DNA stability. Understanding the dysfunction of NTH1 in these contexts helps in exploring potential therapeutic targets and diagnostic markers for related disorders.
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Specifications

Form

Liquid

Additional notes

ab113607 was purified using conventional chromatography.

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General info

Function

Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage (PubMed : 29610152, PubMed : 9927729). The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines. Has also 8-oxo-7,8-dihydroguanine (8-oxoG) DNA glycosylase activity. Acts preferentially on DNA damage opposite guanine residues in DNA. Is able to process lesions in nucleosomes without requiring or inducing nucleosome disruption.

Sequence similarities

Belongs to the Nth/MutY family.

Post-translational modifications

Ubiquitinated by TRIM26; leading to proteasomal degradation.

Subcellular localisation

Nucleus

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Product protocols

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Target data

Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage (PubMed : 29610152, PubMed : 9927729). The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines. Has also 8-oxo-7,8-dihydroguanine (8-oxoG) DNA glycosylase activity. Acts preferentially on DNA damage opposite guanine residues in DNA. Is able to process lesions in nucleosomes without requiring or inducing nucleosome disruption.
See full target information NTHL1
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