| Product Name | SMUG1, 1-270aa, Human |
|---|---|
| Description | Single-strand-selective monofunctional uracil-DNA glycosylase, also known as SMUG1, is a enzyme responsible for recognizing base lesions in the genome and initiating base excision DNA repair. This protein acts as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA and has a preference for single-stranded DNA substrates. Recombinant human SMUG1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Synonyms | Single-strand-selective monofunctional uracil-DNA glycosylase, FDG, HMUDG, UNG3 |
| Host | E. coli |
| Molecular Weight | 27.1kDa (233aa), confirmed by MALDI-TOF |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MGSMPQAFLL GSIHEPAGAL MEPQPCPGSL AESFLEEELR LNAELSQLQF SEPVGIIYNP VEYAWEPHRN YVTRYCQGPK EVLFLGMNPG PFGMAQTGVP FGEVSMVRDW LGIVGPVLTP PQEHPKRPVL GLECPQSEVS GARFWGFFRN LCGQPEVFFH HCFVHNLCPL LFLAPSGRNL TPAELPAKQR EQLLGICDAA LCRQVQLLGV RLVVGVGRLA EQRARRALAG LMPEVQVEGL LHPSPRNPQA NKGWEAVAKE RLNELGLLPL LLK |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl buffer (pH 8.0) containing 0.1M NaCl, 10% glycerol, 1mM DTT |
| Concentration | 1 mg/ml (determined by Bradford assay) |
| Purity | > 95% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Masaoka A., et al. (2003) Biochemistry. 42:5003-5012 Boorstein R.J., et al. (2001) J. Biol. Chem. 276:41991-41997 |
| Background | Single-strand-selective monofunctional uracil-DNA glycosylase, also known as SMUG1, is a enzyme responsible for recognizing base lesions in the genome and initiating base excision DNA repair. This protein acts as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA and has a preference for single-stranded DNA substrates. Recombinant human SMUG1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Supplier | ARP |
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