Recombinant Human Single-Strand Selective Monofunctional Uracil Dna Glycosylase (SMUG1) Protein (His-SUMO)

Name: Recombinant Human Single-Strand Selective Monofunctional Uracil Dna Glycosylase (SMUG1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03206P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Single-Strand Selective Monofunctional Uracil Dna Glycosylase (SMUG1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q53HV7
Target Symbol	SMUG1
Synonyms	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)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MPQAFLLGSIHEPAGALMEPQPCPGSLAESFLEEELRLNAELSQLQFSEPVGIIYNPVEYAWEPHRNYVTRYCQGPKEVLFLGMNPGPFGMAQTGVPFGEVSMVRDWLGIVGPVLTPPQEHPKRPVLGLECPQSEGPRQSMGHEIKSELLMGGCSWIRGKIQCDRVQVRRPGFSSQL
Expression Range	1-177aa
Protein Length	Full Length of Isoform 2
Mol. Weight	35.6kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Nucleus.
Protein Families	Uracil-DNA glycosylase (UDG) superfamily, SMUG1 family
Database References	HGNC: 17148 OMIM: 607753 KEGG: hsa:23583 STRING: 9606.ENSP00000338606 UniGene: Hs.632721

Gene Functions References

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
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
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
Single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) deficiency is linked to aggressive breast cancer and predicts response to adjuvant therapy. PMID: 24253812
The results obtained suggest the potential role of the g.4235T>C and the c.-31A>G polymorphisms in AMD pathogenesis. PMID: 23714858
There was no difference between SMUG1 proficient and depleted cells following continuous exposure. PMID: 23253900
SMUG1 is a DKC1 interaction partner that contributes to rRNA quality control, partly by regulating 5-hydroxymethyluridine levels. PMID: 23246433
Data show that uracil-DNA glycosylases SMUG1 and UNG2 display widely different sequence preferences. PMID: 22483865
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
analysis of species specific differences between mouse and humans in regulation of SMUG1 and UNG2 PMID: 21454529
hSMUG1 is a broad specificity backup for hUNG2, the major enzyme for removal of deaminated cytosine in single strnaded DNA PMID: 12161446
This enzyme has a role in repair of 5-formyluracil and other oxidized and deaminated base lesions. PMID: 12718543
The structure and specificity of SMUG1 have been solved. PMID: 12820976
Site-directed mutagenesis was used to determine the catalytic and DNA damage-recognition mechanism of hSMUG1. PMID: 15466595
SMUG1 plays little natural role in antibody diversification. PMID: 16407970
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
Analysis of the catalytic and precision damage recognition mechanisms of SMUG1. PMID: 17150750
SMUG1 and UNG2 coordinate the initial steps in base excision repair of U:G mismatches by different molecular mechanisms. PMID: 17537817
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
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
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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.