Analytical Data
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Gene name
MPN_142
- Application
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Alternative Names
ORF-3 protein
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Species
Mycoplasma pneumoniae
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q50341
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Expression Region
487-718aa
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Molecular Weight
32.5 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
MPN_142 is a recombinant protein that has garnered attention in the field of molecular biology and protein engineering due to its unique structural and functional properties. Derived from a specific microorganism, MPN_142 plays a crucial role in various biochemical processes, making it a candidate for studies related to enzyme functions, metabolic pathways, and potential applications in biotechnology. The increasing need for sustainable bioprocesses has propelled research into microbial proteins, including MPN_142, to explore their usability in industrial applications such as biocatalysis, biofuels, and pharmaceuticals. Understanding the mechanisms behind MPN_142's activity could provide insights into the evolutionary adaptations of microorganisms to their environments, further advancing our knowledge in synthetic biology. Investigating this protein's properties, such as stability, catalytic efficiency, and interaction with substrates, is essential for developing novel applications that leverage its capabilities in innovative ways. Studies also aim to optimize recombinant expression systems to produce MPN_142 in sufficient quantities for detailed analysis, thereby enhancing its relevance in both academic and commercial research settings. As the demand for efficient and eco-friendly solutions grows, focusing on proteins like MPN_142 represents a promising avenue for future discoveries in the life sciences.
