Analytical Data
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Gene name
ler
- Application
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Alternative Names
/
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Species
Lysobacter enzymogenes
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O87544
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Expression Region
220-463aa
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Molecular Weight
52.7 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 LER (Lipid-Embedded Receptor) recombinant proteins is a burgeoning field in molecular biology, primarily due to the increasing recognition of membrane proteins as crucial players in various biological processes. Membrane proteins, including receptors, transporters, and channels, are integral to cell signaling, homeostasis, and communication. LERs are particularly interesting because they are embedded in lipid membranes, where their structural and functional dynamics differ significantly from those of soluble proteins. The challenge in studying LERs lies in their complex folding, stability, and the difficulty of expressing them in heterologous systems. Advancements in recombinant DNA technology and protein engineering have allowed researchers to design and produce LERs in controlled environments, facilitating the investigation of their structure-function relationships. These studies are essential for understanding how LERs interact with ligands, dictate cellular responses, and contribute to diseases such as cancer and neurological disorders. Furthermore, LERs are potential targets for drug development, providing avenues for the design of innovative therapeutics that can modulate their activity. The integration of techniques such as high-throughput screening, cryo-electron microscopy, and advanced biophysical methods is enhancing our ability to characterize LERs in detail, thus paving the way for new discoveries that could revolutionize our approach to treating various health conditions.
