Analytical Data
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Gene name
MUTYH
- Application
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Alternative Names
MYH; A/G-specific adenine DNA glycosylase
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Species
Human
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Source
E. coli
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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
Q9UIF7
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Expression Region
Gly351~Ala544
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Molecular Weight
28kDa
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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
MUTYH is a DNA glycosylase that plays a crucial role in the base excision repair (BER) pathway, specifically targeting oxidatively damaged DNA bases, such as 8-oxoguanine. Mutations in the MUTYH gene are linked to a genetic disorder known as MUTYH-associated polyposis (MAP), which predisposes individuals to colorectal cancer. The understanding of MUTYH's function is vital for elucidating the mechanisms of DNA repair and its implications in cancer development. Research has shown that decreased or dysfunctional MUTYH activity can lead to the accumulation of mutations, thereby increasing the risk of tumorigenesis. Recombination proteins derived from MUTYH are valuable for studying the enzyme's properties, interactions, and repair mechanisms at a molecular level. Moreover, the expression and reconstitution of recombinant MUTYH proteins allow for the exploration of potential therapeutic targets and biomarkers in colorectal cancer screening and prevention. Continued research into MUTYH and its biochemical pathways is essential for developing targeted therapies and improving risk assessment for individuals carrying pathogenic mutations, thus enhancing our understanding of cancer genomics and precision medicine.
