Recombinant Human Endonuclease III-like protein 1 (NTHL1)

Code CSB-YP016125HU
MSDS
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Source Yeast
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Code CSB-EP016125HU
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Source E.coli
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Code CSB-EP016125HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP016125HU
MSDS
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Source Baculovirus
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Code CSB-MP016125HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
NTHL1
Uniprot No.
Alternative Names
Bifunctional DNA N glycoslyase/DNA (apurinic or apyrimidinic site) lyase; DNA glycoslyase/AP lyase; Endonuclease III like protein 1; Endonuclease III-like protein 1; hNTH1; NTH 1; nth endonuclease III like 1 (E. coli); NTH endonuclease III Like 1; NTH1; NTHL 1; Nthl1; NTHL1_HUMAN; OCTS 3; OCTS3
Species
Homo sapiens (Human)
Expression Region
1-312
Target Protein Sequence
MCSPQESGMT ALSARMLTRS RSLGPGAGPR GCREEPGPLR RREAAAEARK SHSPVKRPRK AQRLRVAYEG SDSEKGEGAE PLKVPVWEPQ DWQQQLVNIR AMRNKKDAPV DHLGTEHCYD SSAPPKVRRY QVLLSLMLSS QTKDQVTAGA MQRLRARGLT VDSILQTDDA TLGKLIYPVG FWRSKVKYIK QTSAILQQHY GGDIPASVAE LVALPGVGPK MAHLAMAVAW GTVSGIAVDT HVHRIANRLR WTKKATKSPE ETRAALEEWL PRELWHEING LLVGFGQQTC LPVHPRCHAC LNQALCPAAQ GL
Protein Length
Full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

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. 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.
Gene References into Functions
  1. The processing of the lesions was evaluated by purified enzyme cocktails of hNTH1 and hOGG1 as well as with a HeLa cell extract. Interestingly, the yield of double-strand breaks (DSBs) resulting from the processing of the bistranded lesions are appreciably lower when the DNA is treated with the HeLa cell extract compared with the relevant purified enzyme cocktail in both models PMID: 30207305
  2. NTHL1 in these extracts was able to excise thymine glycol from both naked DNA and sites in nucleosomes that earlier studies had shown to be sterically accessible. However, the same extracts were able to excise lesions from sterically-occluded sites in nucleosomes only after the addition of Mg2+/ATP. PMID: 28709015
  3. WT NTHL1 (human) and Nth (E. coli) are remarkably alike with respect to specificity of glycosylase reaction, and although NTHL1 is a much slower enzyme than Nth, the tighter binding of NTHL1 compensates, resulting in similar kcat/Kd values for both enzymes with each of the substrates tested. For NTHL1 Gln287Ala, specificity for substrates positioned opposite G is lost, but not that of substrates positioned opposite A. PMID: 28292631
  4. We therefore found published evidence to support the association between variants in NTHL1 and RPS20 with CRC. PMID: 27713038
  5. Both Ntg1 and its human homologue, NTHL1, can be SUMO-modified in response to oxidative stress. PMID: 27839712
  6. NTH1 polymorphisms may be associated with non-small cell lung cancer pathogenesis. PMID: 26400813
  7. This study extends the description of biallelic mutations in NTHL1 beyond the single c.268C-->T,p.Q90* mutation that was observed previously. PMID: 26559593
  8. A homozygous loss-of-function germline mutation in the NTHL1 gene predisposes to a new subtype of BER-associated adenomatous polyposis and colorectal cancer. PMID: 25938944
  9. we demonstrated that hNEIL1 and hNTH1 cleave Oz sites as efficiently as 5-hydroxyuracil sites. Thus, hNEIL1 and hNTH1 can repair Oz lesions PMID: 22465744
  10. NTH1 is involved in removal of 8-oxoguanine from 8-oxoguanine/guanine mispairs in DNA PMID: 11328882
  11. recombinant hNTH1 lacking 55, 72 or 80 residues from the N terminus had four- to fivefold higher activities than the full-length enzyme PMID: 12144783
  12. substrate selectivity of mammalian NTH1 and the concomitant selective stimulation of activity by APE1 are indicative of selective repair of oxidative damage in different regions of the genome PMID: 12519758
  13. dimerization of hNTH1 involving the N-terminal tail masks the inhibitory effect of this tail and plays a critical role in its catalytic turnover in the cell PMID: 14522981
  14. hNTH1 and hNEIL1 but not hNEIL2 excised the two stereoisomers of thymine glycol (5R-Tg and 5S-Tg), but their isomer specificity was markedly different PMID: 14734554
  15. search for the factors interacting with NTH1 shows GST-NTH1 fusion protein precipitates proliferating cell nuclear antigen (PCNA) and p53 as well as XPG from human cell-free extracts PMID: 15358233
  16. NTH1 is a DNA glycosylase that excise 5-formyluracil, 5-hydroxymethyluracil and Thymine glycol in human cells. PMID: 15533839
  17. hNTH1 plays two roles in the processing of radiation damages: repair of potentially lethal single lesions and generation of lethal double strand breaks at clustered damage sites. PMID: 16111924
  18. Nth1 released 5R,6S 2'-deoxyribonucleoside diastereoisomer (Tg2) much more rapidly than cis 5S,6R-deoxyribonucleoside diastereoisomer (Tg1) regardless of the opposing purine. Neil1 released Thymine glycol non-stereoselectively. PMID: 16446124
  19. The damage specificity of human homologues of Endo III (hNTHl) and Endo VIII (hNEIL1 and hNEIL2) is compared to elucidate the repair role in cells. PMID: 17150535
  20. These observations suggest that access to sterically occluded lesions entails the partial, reversible unwrapping of DNA from the histone octamer, allowing hNTH1 to capture its DNA substrate when it is in an unwound state. PMID: 17923696
  21. Downregulation of NTH1 is associated with gastric cancer. PMID: 19414504

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Involvement in disease
Familial adenomatous polyposis 3 (FAP3)
Subcellular Location
Nucleus. Mitochondrion.
Protein Families
Nth/MutY family
Tissue Specificity
Widely expressed with highest levels in heart and lowest levels in lung and liver.
Database Links

HGNC: 8028

OMIM: 602656

KEGG: hsa:4913

STRING: 9606.ENSP00000219066

UniGene: Hs.66196

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