Analytical Data
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Gene name
mleA
- Application
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Alternative Names
mleA；Malolactic enzyme
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
IQGTGIVVLAGVLGALKISGQKLTDQTYMSFGAGTAGMGIVKQLHEEMVEQGLSDEEAKKHFFLVDKQGLLFDDDPDLTPEQKPFAAKRSDFKNANQLTNLQAAVEAVHPTILVGTSTHPNSFTEEIVKDMSGYTERPIIFPISNPTKLAEAKAEDVLKWSNGKALIGTGVPVDDIEYEGNAYQIGQANNALIYPGLGFGAIAAQSKLLTPEMISAAAHSLGGIVDTTKVGAAVLPPVSKLADFSRTVAVAVAKKAV
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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 recombinant protein MleA has gained considerable attention in recent years due to its role in the field of molecular biology and biochemistry. MleA is a regulator involved in various cellular processes, particularly in the context of stress responses and metabolic regulation in microorganisms. Research has shown that MleA is crucial for understanding the mechanisms of gene expression and cellular adaptation to environmental challenges. The ability to produce MleA as a recombinant protein allows for detailed structural and functional studies, facilitating insights into its interaction with other biomolecules and its role in the regulatory networks of cells. Furthermore, the recombinant form of MleA can be utilized in various applications, including drug discovery, where it may serve as a target for designing new therapeutics aimed at diseases where MleA is implicated. The ongoing exploration of MleA not only enhances our understanding of fundamental biological processes but also opens avenues for innovative biotechnological applications, highlighting the importance of recombinant protein research in addressing both scientific questions and practical challenges.
