Analytical Data
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Gene name
Mutc
- Application
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Alternative Names
Methylmalonyl-CoA isomerase
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Species
Mouse
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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
P16332
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Expression Region
31-748aa
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Molecular Weight
83.2 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
MutC protein, a critical component of bacterial DNA repair mechanisms, has garnered significant research interest due to its role in the maintenance of genomic integrity. In Escherichia coli, the MutC protein is part of the methyl-directed mismatch repair (MMR) system, which corrects base-pairing errors that occur during DNA replication. Deficiencies in this system can lead to increased mutation rates, contributing to bacterial resistance and the development of various diseases. Understanding the structure and function of MutC is vital for elucidating the pathways involved in DNA repair and the broader implications for microbial pathogenesis. Recent studies have focused on the biochemical properties and interactions of MutC with other repair proteins, providing insights into its mechanisms of action. Moreover, the potential to manipulate MutC activity presents opportunities for novel therapeutic strategies against antibiotic-resistant bacteria. Research into MutC not only enhances our comprehension of fundamental biological processes but also contributes to the development of innovative interventions in medical microbiology, emphasizing the relevance of this protein in both basic and applied sciences.
