Analytical Data
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Gene name
MutT
- Application
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Alternative Names
7,8-dihydro-8-oxoguanine-triphosphatase;Mutator protein MutTdGTP pyrophosphohydrolase
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Species
Escherichia coli
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08337
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Expression Region
1-129aa
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Molecular Weight
16.9 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
Related Products
Protein Description
MutT is an essential enzyme involved in maintaining genomic stability by preventing the incorporation of oxidized nucleotides into DNA. Its primary function is to hydrolyze 8-oxo-deoxyguanosine triphosphate (8-oxo-dGTP), a prevalent lesion generated by oxidative stress, into its non-canonical form, thereby averting potential mutagenesis during DNA replication. The significance of MutT extends beyond simple nucleotide protection; it also plays a critical role in various cellular processes, including DNA repair, replication fidelity, and overall cellular response to oxidative damage. Understanding the structure and function of MutT has garnered considerable attention due to its implications in cancer biology and aging, where oxidative DNA damage is a common factor. Researchers have focused on the enzymatic mechanisms, substrate specificity, and regulatory pathways of MutT, utilizing various biochemical and molecular biology techniques. The elucidation of MutT's role in cellular defense mechanisms against oxidative stress contributes to broader insights into how organisms preserve genetic integrity and respond to environmental challenges. As a result, investigations into MutT not only enhance our understanding of fundamental biological processes but also open avenues for potential therapeutic strategies in diseases characterized by oxidative damage.
