NTH (AA 1-211) protein (His tag)
Origin: E. coli
Host: Escherichia coli (E. coli)
Recombinant
> 90% by SDS-PAGE
SDS
1 image
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- Target
- NTH
- Protein Type
- Recombinant
- Protein Characteristics
- AA 1-211
- Origin
- E. coli
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Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- His tag
- Application
- SDS-PAGE (SDS)
- Sequence
- MGSSHHHHHH SSGLVPRGSH MNKAKRLEIL TRLRENNPHP TTELNFSSPF ELLIAVLLSA QATDVSVNKA TAKLYPVANT PAAMLELGVE GVKTYIKTIG LYNSKAENII KTCRILLEQH NGEVPEDRAA LEALPGVGRK TANVVLNTAF GWPTIAVDTH IFRVCNRTQF APGKNVEQVE EKLLKVVPAE FKVDCHHWLI LHGRYTCIAR KPRCGSCIIE DLCEYKEKVD I
- Characteristics
- nth, 1-211aa, E.coli, His tag, E.coli
- Purity
- > 90% by SDS-PAGE
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- Application Notes
- Optimal working dilution should be determined by the investigator.
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 0.25 mg/mL
- Buffer
- Liquid. 20mM Tris-HCl buffer (pH8.0) containing 40% glycerol, 0.1M NaCl, 1mM DTT, 0.1mM PMSF
- Storage
- 4 °C,-20 °C,-80 °C
- Storage Comment
- Can be stored at +2°C to +8°C for 1 week. For long term storage, aliquot and store at -20°C to -80°C. Avoid repeated freezing and thawing cycles.
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- Target
- NTH
- Background
- Endonuclease III, also known as nth, is a DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. Recombinant E. coli nth protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography.
- Molecular Weight
- 25.7 kDa (231aa) confirmed by MALDI-TOF
- NCBI Accession
- NP_416150
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