Analytical Data
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Gene name
MPN_311
- Application
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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
P75470
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Expression Region
1-357aa
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Molecular Weight
48.0 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 MPN_311 recombinant protein has gained significant attention in recent years due to its potential applications in biotechnology and medicine. Initially identified in specific bacterial strains, MPN_311 is believed to play a crucial role in various biological processes, possibly related to stress response and metabolic regulation. The recombinant form of this protein allows researchers to explore its structural and functional properties in a controlled environment, facilitating a deeper understanding of its mechanisms. Advances in genetic engineering techniques, such as CRISPR and plasmid-based expression systems, have enabled the efficient production of MPN_311, paving the way for subsequent analyses including protein folding, activity assays, and interaction studies with other biomolecules. Furthermore, the insights gained from studying MPN_311 could lead to innovations in therapeutic interventions, particularly in addressing diseases linked to protein misfolding and aggregation. Overall, the exploration of MPN_311 recombinant protein represents a significant step towards unraveling complex biological pathways and harnessing the therapeutic potential of proteins in clinical applications.
