Recombinant Human Single-strand selective monofunctional uracil DNA glycosylase (SMUG1)

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Code CSB-EP706636HU
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Size $224
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
SMUG1
Uniprot No.
Research Area
Epigenetics and Nuclear Signaling
Alternative Names
FDG; HMUDG; MGC104370; Single strand selective monofunctional uracil DNA glycosylase 1; Single strand selective monofunctional uracil DNA glycosylase; Single-strand selective monofunctional uracil DNA glycosylase; SMUG 1; Smug1; SMUG1 protein; SMUG1_HUMAN; UNG 3; UNG3
Species
Homo sapiens (Human)
Source
E.coli
Expression Region
1-177aa
Target Protein Sequence
MPQAFLLGSIHEPAGALMEPQPCPGSLAESFLEEELRLNAELSQLQFSEPVGIIYNPVEYAWEPHRNYVTRYCQGPKEVLFLGMNPGPFGMAQTGVPFGEVSMVRDWLGIVGPVLTPPQEHPKRPVLGLECPQSEGPRQSMGHEIKSELLMGGCSWIRGKIQCDRVQVRRPGFSSQL
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
35.6kDa
Protein Length
Full Length of Isoform 2
Tag Info
N-terminal 6xHis-SUMO-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

Amino acids 1-177 constitute the expression domain of recombinant Human SMUG1. This SMUG1 protein is expected to have a theoretical molecular weight of 35.6 kDa. Expression of this SMUG1 protein is conducted in e.coli. Fusion of the N-terminal 6xHis-SUMO tag into the SMUG1 encoding gene fragment was conducted, allowing for easier detection and purification of the SMUG1 protein in subsequent stages.

Human single-strand selective monofunctional uracil DNA glycosylase (SMUG1) is a DNA repair enzyme crucial for base excision repair. SMUG1 specifically recognizes and removes uracil from single-stranded DNA, preventing mutagenesis. In genomics, SMUG1 is essential for maintaining genome integrity and stability. Research on SMUG1 extends to immunology, where it influences somatic hypermutation during antibody maturation. Additionally, SMUG1 is implicated in neurobiology, playing a role in oxidative DNA damage repair in neurons. Investigating SMUG1 provides insights into DNA repair mechanisms, genomic stability, and disease susceptibility, offering potential applications in understanding and preventing mutagenic events, as well as implications for immunology and neurological disorders.

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Target Background

Function
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.
Gene References into Functions
  1. This analysis showed a relative increase in the expression of E2F6 in gastric adenocarcinoma with no lymph node metastasis (chi (2), P = 0.04 and OR, P = 0.08), while overexpression of RhoA and SMUG1 was found more often in the diffuse subtype of gastric adenocarcinoma as compared to the intestinal subtype. PMID: 27909884
  2. Our study showed that c.-31A/G-SMUG1 genotypes/alleles do not have any association with the occurrence or severity of advanced type age-related macular degeneration (AMD). There was no interaction of CRP levels and SMUG1 genotypes in AMD susceptibility. PMID: 28095127
  3. A case-control study of 801 bladder cancer patients and 801 matched controls, the associations of 167 single nucleotide polymorphisms (SNPs) from 19 genes of the BER pathway with the risk of bladder cancer; 13 SNPs in 10 Base excision repair (BER) pathway genes were significantly associated with bladder cancer risk; most significant SNP was rs2029167 in the SMUG1 gene. PMID: 24038406
  4. Single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) deficiency is linked to aggressive breast cancer and predicts response to adjuvant therapy. PMID: 24253812
  5. The results obtained suggest the potential role of the g.4235T>C and the c.-31A>G polymorphisms in AMD pathogenesis. PMID: 23714858
  6. There was no difference between SMUG1 proficient and depleted cells following continuous exposure. PMID: 23253900
  7. SMUG1 is a DKC1 interaction partner that contributes to rRNA quality control, partly by regulating 5-hydroxymethyluridine levels. PMID: 23246433
  8. Data show that uracil-DNA glycosylases SMUG1 and UNG2 display widely different sequence preferences. PMID: 22483865
  9. there was increased risk of breast cancer among postmenopausal women heterozygous for either SMUG1 rs2029166 or rs7296239. Among premenopausal women, the increased risk associated with SMUG1 rs2029166 was limited to those with low folate intake. PMID: 21427733
  10. analysis of species specific differences between mouse and humans in regulation of SMUG1 and UNG2 PMID: 21454529
  11. hSMUG1 is a broad specificity backup for hUNG2, the major enzyme for removal of deaminated cytosine in single strnaded DNA PMID: 12161446
  12. This enzyme has a role in repair of 5-formyluracil and other oxidized and deaminated base lesions. PMID: 12718543
  13. The structure and specificity of SMUG1 have been solved. PMID: 12820976
  14. Site-directed mutagenesis was used to determine the catalytic and DNA damage-recognition mechanism of hSMUG1. PMID: 15466595
  15. SMUG1 plays little natural role in antibody diversification. PMID: 16407970
  16. A G44T missense mutation was found in familial colorectal cancer DNA suggesting a limited role for this gene in the devlopment of CRC. PMID: 17029639
  17. Analysis of the catalytic and precision damage recognition mechanisms of SMUG1. PMID: 17150750
  18. SMUG1 and UNG2 coordinate the initial steps in base excision repair of U:G mismatches by different molecular mechanisms. PMID: 17537817
  19. proline substitution at the G63 position switches the Gme SMUG1 enzyme to an exclusive UDG as demonstrated by the uniform excision of uracil in both double-stranded and single-stranded DNA and the complete loss of XDG activity PMID: 18835277
  20. Properties used by hSMUG1 to select damaged pyrimidines include the size and free energy of solvation of the 5-substituent but not electronic inductive properties. PMID: 19324873
  21. hSMUG1 excised fU from DNA opposite all normal bases with the highest activity when opposite non-cognate C or T followed by G and cognate A PMID: 19365746

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Subcellular Location
Nucleus.
Protein Families
Uracil-DNA glycosylase (UDG) superfamily, SMUG1 family
Database Links

HGNC: 17148

OMIM: 607753

KEGG: hsa:23583

STRING: 9606.ENSP00000338606

UniGene: Hs.632721

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