Analytical Data
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Gene name
mppA
- Application
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Alternative Names
mppA; ynaH; b1329; JW1322; Periplasmic murein peptide-binding protein
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P77348
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Expression Region
23-537aa
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Molecular Weight
73.6 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
The study of MppA recombinant protein has gained significant attention in the field of microbiology and biotechnology due to its roles in microbial metabolism and potential applications in industrial processes. MppA, a membrane-associated protein, is implicated in the transport and metabolism of various metabolites, particularly in bacteria that exhibit unique adaptations to their environments. Research has highlighted its involvement in critical cellular functions such as nutrient acquisition, stress response, and cell signaling. Advances in genetic engineering and recombinant DNA technology have facilitated the production of MppA in heterologous systems, allowing for detailed functional studies and structural characterization. Understanding the molecular mechanisms of MppA can provide insights into the evolutionary significance of membrane proteins and their exploitation in biotechnology, such as biosensors, biocatalysts, and bioengineering applications. The exploration of MppA also promises to enhance our comprehension of pathogenic mechanisms in specific bacteria, potentially guiding antibiotic development and improving microbial bioremediation strategies. As such, MppA stands at the intersection of basic research and practical applications, making it a significant focus for ongoing studies aimed at harnessing microbial diversity for technological innovations.
