e.coli nth protein (Recombinant) (His-Tag) (STJP017187)
SPECIFICATIONS
HostE.coli
ImmunogenE.coli
General Information
| Short Description | Recombinant-e.coli nth-His-Tag protein was developed from e.coli and has a target region of His-Tag. For use in research applications. |
| Applications | SDS-PAGE |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Concentration | 0.25 mg/mL |
| Formulation | Liquid in 20mM Tris-HCl buffer (pH 8.0) containing 40% Glycerol, 0.1M NaCl, 1mM DTT, 0.1mM PMSF |
| Storage Instruction | For short term storage, keep at +2C to +8C for up to 1 week. For long term storage, aliquot and store at-20C, and avoid repeat freeze-thaw cycles. |
Target Information
| Accession Number | NP_416150 |
| Immunogen | E.coli |
| Immunogen Region | 1-211aa |
| Immunogen Sequence | MGSSHHHHHH SSGLVPRGSH MNKAKRLEIL TRLRENNPHP TTELNFSSPF ELLIAVLLSA QATDVSVNKA TAKLYPVANT PAAMLELGVE GVKTYIKTIG LYNSKAENII KTCRILLEQH NGEVPEDRAA LEALPGVGRK TANVVLNTAF GWPTIAVDTH IFRVCNRTQF APGKNVEQVE EKLLKVVPAE FKVDCHHWLI LHGRYTCIAR KPRCGSCIIE DLCEYKEK |
Additional Info
| 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 NA-terminal unsaturated sugar and a product with a terminal 5 NA-phosphate. Recombinant E. coli nth protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography. |
Information sourced from Uniprot.org