Analytical Data
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Gene name
lacY
- Application
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Alternative Names
Lactose-proton symport
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Species
Escherichia coli
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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
P02920
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Expression Region
1-250aa
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Molecular Weight
34.4 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
The study of the lacY gene, which encodes the lactose permease protein in Escherichia coli, has garnered significant attention due to its essential role in carbohydrate transport and metabolic regulation. Lactose permease facilitates the symport of lactose and protons across the bacterial membrane, a process crucial for E. coli's ability to utilize lactose as a carbon source. This protein is a member of the major facilitator superfamily (MFS) and serves as a model for understanding membrane protein function and transport mechanisms. The study of lacY has important implications for biotechnology and medicine, particularly in improving lactose utilization in dairy products and understanding antibiotic resistance mechanisms. Recent advances in structural biology, including X-ray crystallography and cryo-electron microscopy, have provided insights into the dynamic nature of lacY, revealing conformational changes during the transport cycle. Researchers are also exploring the potential for engineering lacY for enhanced performance in various applications, including metabolic engineering in synthetic biology. Investigating the molecular mechanisms of lacY not only contributes to our fundamental understanding of cellular transport processes but also offers pathways for innovative solutions in industrial biotechnology and health sciences.
