Analytical Data
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Gene name
lacY
- Application
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Alternative Names
lacY；Dymeclin
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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
P02920
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Expression Region
1-250aa
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AA Sequence
MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTGIIFAAISLFSLLFQPLFGLLSDKLGLRKYLLWIITGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFCFNAGAPAVEAFIEKVSRRSNFEFGRARMFGCVGWALCASIVGIMFTINNQFVFWLGSGCALILAVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSCTYDVFDQQFANFFTSF
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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 LacY, the lactose permease of Escherichia coli, has garnered considerable attention due to its pivotal role in nutrient transport and its significance in understanding membrane protein function. LacY functions as a symporter that facilitates the co-transport of lactose and protons across the bacterial membrane, thereby playing a crucial role in the metabolism of lactose. Its ability to transport substrates against their concentration gradient highlights essential mechanisms of active transport and energy coupling. Research into LacY has not only provided insights into the function and structural dynamics of membrane proteins but has also paved the way for understanding similar transport proteins in higher organisms. Recombinant expression of LacY allows for detailed studies of its structure and function, utilizing techniques such as X-ray crystallography and molecular dynamics simulations. These studies have revealed key structural features and conformational changes associated with substrate binding and translocation. Moreover, LacY serves as a model for studying other members of the major facilitator superfamily (MFS), making it an invaluable tool in the field of membrane biology and biochemistry. The advances in LacY research continue to contribute to our understanding of transport mechanisms and hold potential implications for biotechnological applications and drug design.
