Description of target: Recognizes base lesions in the genome and initiates base excision DNA repair. Acts as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA with a preference for single-stranded DNA substrates. The activity is greater toward mismatches (U/G) compared to matches (U/A). Excises uracil (U), 5-formyluracil (fU) and uracil derivatives bearing an oxidized group at C5 [5-hydroxyuracil (hoU) and 5-hydroxymethyluracil (hmU)] in ssDNA and dsDNA, but not analogous cytosine derivatives (5-hydroxycytosine and 5-formylcytosine), nor other oxidized bases. The activity is damage-specific and salt-dependent. The substrate preference is the following: ssDNA > dsDNA (G pair) = dsDNA (A pair) at low salt concentration, and dsDNA (G pair) > dsDNA (A pair) > ssDNA at high salt concentration.4 Publications
 <p>Manually curated information for which there is published experimental evidence.</p>
 
 
 <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment iniRef.1"Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors."_x005F_x005F_x000D_Haushalter K.A., Stukenberg P.T., Kirschner M.W., Verdine G.L._x005F_x005F_x000D_Curr. Biol. 9:174-185(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.Ref.2"Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions."_x005F_x005F_x000D_Masaoka A., Matsubara M., Hasegawa R., Tanaka T., Kurisu S., Terato H., Ohyama Y., Karino N., Matsuda A., Ide H._x005F_x005F_x000D_Biochemistry 42:5003-5012(2003) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.Ref.8"Definitive identification of mammalian 5-hydroxymethyluracil DNA N-glycosylase activity as SMUG1."_x005F_x005F_x000D_Boorstein R.J., Cummings A. Jr., Marenstein D.R., Chan M.K., Ma Y., Neubert T.A., Brown S.M., Teebor G.W._x005F_x005F_x000D_J. Biol. Chem. 276:41991-41997(2001) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 13-21; 26-37; 46-66; 79-105; 124-140; 141-146; 147-157; 188-200; 201-208; 224-243 AND 259-270, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.Ref.9"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."_x005F_x005F_x000D_Kavli B., Sundheim O., Akbari M., Otterlei M., Nilsen H., Skorpen F., Aas P.A., Hagen L., Krokan H.E., Slupphaug G._x005F_x005F_x000D_J. Biol. Chem. 277:39926-39936(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. ;Species reactivity: Human;Application: ELISA;Assay info: Assay Methodology: Quantitative Sandwich Immunoassay;Sensitivity: < 0.051 ng/mL
997.2EUR
Preț : 997.2 €
În stoc
Număr Catalog 247-OKCD00524CategorieAfaceri și industrie > Știință și laboratorFurnizorAviva Systems BiologyGentaurDimensiune96 WellsTipsingle
