Analytical Data
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Gene name
mutS
- Application
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Alternative Names
mutS；MutS Protein homolog 4
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Species
E.coli
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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
Q67NK1
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Expression Region
574-781aa
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AA Sequence
YGYCRPLVDGSTVLELKGSRHPVLERVMEEGAFVPNDLLVDTGENRVLLITGPNMGGKSTVMRQAALAVILAQAGSFVPAESAHIGLVDRVFTRVGASDDLATGRSTFMVEMTEVANILHSATERSLVVLDEVGRGTATFDGLSIAWAITEHIHQAIGCRTLFATHYHELCELEGILPGVKNYSVAVMEKGEDIIFLRKLVRGGADRS
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Molecular Weight
29.4 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
MutS is a key protein involved in the DNA mismatch repair (MMR) system, which is crucial for maintaining genomic stability by correcting base-pair mismatches and insertion-deletion loops that arise during DNA replication and recombination. The discovery of MutS dates back to studies on Escherichia coli, where it was identified as a crucial player in the repair mechanism, recognizing and binding to mismatched DNA. This recognition initiates a cascade of events leading to the repair of erroneous DNA sequences, thereby preventing mutations that could lead to carcinogenesis or other genetic diseases. Research on MutS has expanded to explore its roles in various organisms, including humans, where homologous proteins play similar functions. Understanding the structural and functional dynamics of MutS and its homologs has significant implications for cancer biology, as deficiencies in the MMR system are linked to several hereditary cancer syndromes, such as Lynch syndrome. Furthermore, the study of MutS provides insights into evolutionary conservation mechanisms in DNA repair processes. Recent advancements in techniques like X-ray crystallography and cryo-electron microscopy have facilitated detailed studies of the MutS structure and its interactions with DNA, enhancing our knowledge of the molecular basis of MMR. Through ongoing research, scientists aim to uncover potential therapeutic targets within the MMR pathway to improve cancer treatment strategies and develop novel biomolecular tools for genetic analysis and engineering. Overall, the study of MutS holds promise for enhancing our understanding of genome integrity and the molecular underpinnings of various diseases.
