SMUG1 Protein, Human (His-SUMO)

SMUG1 protein is a single-function DNA glycosylase that plays a crucial role in base excision DNA repair, especially the recognition and repair of uracil (U) residues, preferentially recognizing mismatches (U/G) rather than matching (U/A). Its activity extends to the excision of 5-formyluracil (fU), 5-hydroxyuracil (hoU) and 5-hydroxymethyluracil (hmU) in single-stranded (ssDNA) and double-stranded DNA (dsDNA). SMUG1 Protein, Human (His-SUMO) is the recombinant human-derived SMUG1 protein, expressed by E. coli , with N-His, N-SUMO labeled tag. The total length of SMUG1 Protein, Human (His-SUMO) is 177 a.a., with molecular weight of ~35.6 kDa.

The SMUG1 protein serves as a pivotal factor in base excision DNA repair, specifically recognizing and initiating repair processes for base lesions in the genome. Functioning as a monofunctional DNA glycosylase, SMUG1 displays specificity for uracil (U) residues in DNA, with a notable preference for single-stranded DNA substrates. Its enzymatic activity is more pronounced toward mismatches (U/G) compared to matches (U/A). SMUG1 exhibits the capability to excise not only uracil (U) but also 5-formyluracil (fU), and uracil derivatives with oxidized groups at C5, such as 5-hydroxyuracil (hoU) and 5-hydroxymethyluracil (hmU), in both single-stranded (ssDNA) and double-stranded DNA (dsDNA). Importantly, this DNA glycosylase does not act on analogous cytosine derivatives (5-hydroxycytosine and 5-formylcytosine), nor other oxidized bases. SMUG1's activity is damage-specific and exhibits dependence on salt concentration, with a substrate preference hierarchy of ssDNA > dsDNA (G pair) = dsDNA (A pair) under low salt conditions, and dsDNA (G pair) > dsDNA (A pair) > ssDNA under high salt concentrations.

Human

E. coli

N-His;N-SUMO

Q53HV7 (1M-177L)

23583  [NCBI]

MPQAFLLGSIHEPAGALMEPQPCPGSLAESFLEEELRLNAELSQLQFSEPVGIIYNPVEYAWEPHRNYVTRYCQGPKEVLFLGMNPGPFGMAQTGVPFGEVSMVRDWLGIVGPVLTPPQEHPKRPVLGLECPQSEGPRQSMGHEIKSELLMGGCSWIRGKIQCDRVQVRRPGFSSQL

Approximately 35.6 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.