Analytical Data
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Gene name
mipA
- Application
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Species
Escherichia coli
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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
P0A908
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Expression Region
23-248aa
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Molecular Weight
33.1 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
MipA is a crucial protein involved in the biogenesis of the bacterial ribosome, playing a key role in ribosomal assembly and function. Its significance stems from its involvement in the formation of functional ribosomal subunits, which are essential for protein synthesis in all living organisms. Research into MipA has gained momentum due to the increasing understanding of its structural and functional properties, as well as its potential as a target for novel antibiotic development. With the rise of antibiotic resistance among bacterial pathogens, enzymes and proteins involved in ribosome assembly, such as MipA, are being investigated for their potential as drug targets. Furthermore, MipA's unique structural features and interactions within the ribosomal assembly pathway offer insights into the evolutionary adaptations of bacteria, providing a deeper understanding of microbial life and its mechanisms. Given its critical functions and the challenges associated with antibiotic resistance, studying MipA and its recombinant form is vital for developing new therapeutic strategies and enhancing our comprehension of ribosome biogenesis in both pathogenic and non-pathogenic bacteria. This research could lead to breakthroughs not only in microbiology but also in pharmacology, potentially paving the way for innovative treatments against resistant bacterial strains.
