Analytical Data
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Gene name
SMUG1
- Application
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Alternative Names
SMUG1;Single-strand selective monofunctional uracil DNA glycosylase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q53HV7-2
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Expression Region
1-177aa
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AA Sequence
MPQAFLLGSIHEPAGALMEPQPCPGSLAESFLEEELRLNAELSQLQFSEP VGIIYNPVEYAWEPHRNYVTRYCQGPKEVLFLGMNPGPFGMAQTGVPFGE VSMVRDWLGIVGPVLTPPQEHPKRPVLGLECPQSEGPRQSMGHEIKSELL MGGCSWIRGKIQCDRVQVRRPGFSSQL
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Molecular Weight
46 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
SMUG1 (single-stranded DNA-binding protein 1) is a crucial enzyme involved in the maintenance of genome stability and the repair of damaged DNA. It is classified as a DNA glycosylase, which plays a vital role in the base excision repair (BER) pathway by recognizing and removing oxidized and alkylated DNA bases. Given the increasing understanding of the relationship between DNA damage and various diseases, including cancer, the study of SMUG1 has garnered significant interest. Research has shown that SMUG1 is essential for protecting cells against oxidative stress and maintaining normal cellular functions. Moreover, alterations in SMUG1 activity have been implicated in the sensitivity of cancer cells to certain therapies, highlighting its potential as a therapeutic target. The recombinant expression of SMUG1 protein has become an important area of study, as it provides a means to investigate its structural characteristics, enzymatic activity, and interaction with other cellular components. Advancements in protein purification techniques enable researchers to produce and analyze SMUG1 in vitro, facilitating a deeper understanding of its role in DNA repair mechanisms and its potential implications in cancer biology. Overall, the exploration of SMUG1 and its recombinant protein is pivotal for unveiling new avenues in cancer treatment and enhancing our comprehension of genomic integrity.
