Single-strand selective monofunctional uracil DNA glycosylase Recombinant Protein | SMUG1 recombinant protein

Recombinant Human Single-strand selective monofunctional uracil DNA glycosylase

Cat. Num. AAA9421192

• Gene Names: SMUG1; FDG; UNG3; HMUDG
• Reactivity: Human
• Purity: Greater than 90% as determined by SDS-PAGE.
• Synonyms: Single-strand selective monofunctional uracil DNA glycosylase; Recombinant Human Single-strand selective monofunctional uracil DNA glycosylase; SMUG1 recombinant protein

• Host: E Coli
• Reactivity: Human
• Purity/Purification: Greater than 90% as determined by SDS-PAGE.
• Form/Format: 20mM Tris-HCl based buffer, pH8.0
• Sequence Positions: Full Length of isoform 2, 1-177aa

• Tag Info: His-SUMO-tag
• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C. Repeated freezing and thawing is not recommended. Store working aliquots at 4 degree C for up to one week.

Related Product Information for SMUG1 recombinant protein

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.

NCBI and Uniprot Product Information

• NCBI GI #: 344925869
• NCBI GeneID: 23583
• NCBI Accession #: NP_001230716.1
• NCBI GenBank Nucleotide #: NM_001243787.1
• UniProt Accession #: Q53HV7; O95862; Q0D2M0; Q8NB71; Q9BWC8; A8K2K9
• Molecular Weight: 35.61kD
• NCBI Official Full Name: single-strand selective monofunctional uracil DNA glycosylase isoform 1
• NCBI Official Synonym Full Names: single-strand-selective monofunctional uracil-DNA glycosylase 1
• NCBI Official Symbol: SMUG1
• NCBI Official Synonym Symbols: FDG; UNG3; HMUDG
• NCBI Protein Information: single-strand selective monofunctional uracil DNA glycosylase
• UniProt Protein Name: Single-strand selective monofunctional uracil DNA glycosylase
• Protein Family: Single-strand selective monofunctional uracil DNA glycosylase
• UniProt Gene Name: SMUG1

NCBI Description

This gene encodes a protein that participates in base excision repair by removing uracil from single- and double-stranded DNA. Many alternatively spliced transcript variants exist for this gene; the full-length nature is known for some but not all of the variants. [provided by RefSeq, Aug 2011]

Uniprot Description

SMUG1: Responsible for recognizing base lesions in the genome and initiating base excision DNA repair. Acts as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA and has a preference for single-stranded DNA substrates. The activity is greater against mismatches (U/G) than against matches (U/A). Excised 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) and other oxidized damage. The activity is damage specificity and salt concentration-dependent. The general order of the preference for ssDNA and dsDNA is the following: ssDNA > dsDNA (G pair) = dsDNA (A pair) at the low salt concentration. At the high concentration dsDNA (G pair) > dsDNA (A pair) > ssDNA. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: DNA repair, damage; EC 3.2.2.-; Hydrolase

Chromosomal Location of Human Ortholog: 12q13.13

Cellular Component: nucleolus; nucleoplasm

Molecular Function: DNA N-glycosylase activity; oxidized pyrimidine base lesion DNA N-glycosylase activity; protein binding; single-strand selective uracil DNA N-glycosylase activity; uracil DNA N-glycosylase activity

Biological Process: base-excision repair; depyrimidination