Analytical Data
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Gene name
MUTYH
- Application
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Alternative Names
MUTYH;MYH;Adenine 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
P17802
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Expression Region
1-350aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMQASQFS AQVLDWYDKY GRKTLPWQID KTPYKVWLSE VMLQQTQVAT VIPYFERFMA RFPTVTDLAN APLDEVLHLW TGLGYYARAR NLHKAAQQVA TLHGGKFPET FEEVAALPGV GRSTAGAILS LSLGKHFPIL DGNVKRVLAR CYAVSGWPGK KEVENKLWSL SEQVTPAVGV ERFNQAMMDL GAMICTRSKP KCSLCPLQNG CIAAANNSWA LYPGKKPKQT LPERTGYFLL LQHEDEVLLA QRPPSGLWGG LYCFPQFADE ESLRQWLAQR QIAADNLTQL TAFRHTFSHF HLDIVPMWLP VSSFTGCMDE GNALWYNLAQ PPSVGLAAPV ERLLQQLRTG APV
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Molecular Weight
42 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
MUTYH (MutY human homolog) is an essential DNA repair enzyme that plays a crucial role in maintaining genomic stability by recognizing and excising adenine mispairs that arise during DNA replication, particularly those caused by oxidative damage. Defects in the MUTYH gene can lead to MUTYH-associated polyposis (MAP), a hereditary condition characterized by an increased risk of colorectal cancer and the development of numerous adenomatous polyps. Understanding the structure and function of MUTYH is vital for elucidating its role in the base excision repair pathway and its implications in cancer predisposition. Recent studies have focused on the recombinant expression of MUTYH protein to analyze its enzymatic activity, binding mechanisms, and interactions with other repair proteins. Advanced techniques such as X-ray crystallography and cryo-electron microscopy have provided insights into the protein's structure, revealing critical sites for substrate recognition and enzyme catalysis. Investigating the biochemical properties of MUTYH and the consequences of its mutations allows researchers to develop potential targeted therapies and genetic screening tools for individuals at risk, thereby paving the way for improved prevention strategies in colorectal cancer. The ongoing research highlights the significance of MUTYH in both fundamental biology and clinical applications, reinforcing its potential as a target for therapeutic intervention in DNA repair-related disorders.
