SMUG1 is a glycosylase that removes uracil from single- and double-stranded DNA in nuclear chromatin, thus contributing to base excision repair. The deduced 270-amino acid protein has a calculated molecular mass of about 30 kD. Human SMUG1 shares 60% identity with the Xenopus protein. Fluorescence-tagged SMUG1 localized predominantly to the nucleus of transiently transfected HeLa cells.
SMUG1 showed broader substrate specificity than UNG2, and AP endonuclease had a strong stimulatory effect on SMUG1 against double-stranded uracil, apparently due to enhance dissociation of SMUG1 from AP sites in double-stranded DNA. SMUG1 accumulated within nucleoli in cultured epithelial cells, while UNG2 was excluded from nucleoli.
Organism species: Homo sapiens (Human)
CATALOG NO. | PRODUCT NAME | APPLICATIONS | |
Proteins | RPH164Hu01 | Recombinant Single Strand Selective Monofunctional Uracil DNA Glycosylase 1 (SMUG1) | Positive Control; Immunogen; SDS-PAGE; WB. |
Antibodies | PAH164Hu01 | Polyclonal Antibody to Single Strand Selective Monofunctional Uracil DNA Glycosylase 1 (SMUG1) | WB; IHC; ICC; IP. |
MAH164Hu21 | Monoclonal Antibody to Single Strand Selective Monofunctional Uracil DNA Glycosylase 1 (SMUG1) | WB; IHC; ICC; IP. | |
Assay Kits | SEH164Hu | ELISA Kit for Single Strand Selective Monofunctional Uracil DNA Glycosylase 1 (SMUG1) | Enzyme-linked immunosorbent assay for Antigen Detection. |
Organism species: Mus musculus (Mouse)
CATALOG NO. | PRODUCT NAME | APPLICATIONS | |
Proteins | n/a | Recombinant Single Strand Selective Monofunctional Uracil DNA Glycosylase 1 (SMUG1) | Recombinant Protein Customized Service Offer |
Antibodies | n/a | Monoclonal Antibody to Single Strand Selective Monofunctional Uracil DNA Glycosylase 1 (SMUG1) | Monoclonal Antibody Customized Service Offer |
n/a | Polyclonal Antibody to Single Strand Selective Monofunctional Uracil DNA Glycosylase 1 (SMUG1) | Polyclonal Antibody Customized Service Offer | |
Assay Kits | n/a | CLIA Kit for Single Strand Selective Monofunctional Uracil DNA Glycosylase 1 (SMUG1) | CLIA Kit Customized Service Offer |
n/a | ELISA Kit for Single Strand Selective Monofunctional Uracil DNA Glycosylase 1 (SMUG1) | ELISA Kit Customized Service Offer |
Organism species: Rattus norvegicus (Rat)
CATALOG NO. | PRODUCT NAME | APPLICATIONS | |
Proteins | n/a | Recombinant Single Strand Selective Monofunctional Uracil DNA Glycosylase 1 (SMUG1) | Recombinant Protein Customized Service Offer |
Antibodies | n/a | Monoclonal Antibody to Single Strand Selective Monofunctional Uracil DNA Glycosylase 1 (SMUG1) | Monoclonal Antibody Customized Service Offer |
n/a | Polyclonal Antibody to Single Strand Selective Monofunctional Uracil DNA Glycosylase 1 (SMUG1) | Polyclonal Antibody Customized Service Offer | |
Assay Kits | n/a | CLIA Kit for Single Strand Selective Monofunctional Uracil DNA Glycosylase 1 (SMUG1) | CLIA Kit Customized Service Offer |
n/a | ELISA Kit for Single Strand Selective Monofunctional Uracil DNA Glycosylase 1 (SMUG1) | ELISA Kit Customized Service Offer |
- "Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors."Curr. Biol. 9:174-185(1999) [PubMed] [Europe PMC] [Abstract]
- "Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions."Biochemistry 42:5003-5012(2003) [PubMed] [Europe PMC] [Abstract]
- "Complete sequencing and characterization of 21,243 full-length human cDNAs." Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
- "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
- "Definitive identification of mammalian 5-hydroxymethyluracil DNA N-glycosylase activity as SMUG1."J. Biol. Chem. 276:41991-41997(2001) [PubMed] [Europe PMC] [Abstract]
- "hUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup."J. Biol. Chem. 277:39926-39936(2002) [PubMed] [Europe PMC] [Abstract]
- "Mutational analysis of the damage-recognition and catalytic mechanism of human SMUG1 DNA glycosylase."Nucleic Acids Res. 32:5291-5302(2004) [PubMed] [Europe PMC] [Abstract]