Analytical Data
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Gene name
mleA
- Application
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Alternative Names
(MLE)
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Species
Oenococcus oeni
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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
Q48796
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Expression Region
260-516aa
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Molecular Weight
31.2 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
Related Products
Protein Description
The study of MleA recombinant protein has garnered significant interest due to its potential role in various biological processes and applications in biotechnology. MleA, originally identified in certain bacterial species, is believed to be involved in the regulation of gene expression and metabolic pathways. Its unique structural features suggest that it may interact with various biomolecules, influencing cellular functions. Research has shown that MleA exhibits potential as a target for antibiotic development, especially against drug-resistant strains, due to its critical role in bacterial survival. Additionally, MleA's ability to form complexes with other proteins opens avenues for its application in synthetic biology, where it could be engineered for enhanced functionalities. Scientists are also investigating the recombinant expression of MleA to explore its biochemical properties and functional mechanisms in vitro, which could provide insights into its role in pathogenesis and cellular metabolism. Thus, understanding the dynamics of MleA can pave the way for novel therapeutic strategies and biotechnological innovations, making it a focal point of current research in microbiology and molecular biology.
