Analytical Data
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Gene name
LBP
- Application
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Alternative Names
LPS-Binding Protein
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q63313
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Expression Region
Leu226~Arg481
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Molecular Weight
34kDa
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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 LBP (Lipid-binding protein) recombinant proteins has gained significant attention due to their crucial role in lipid metabolism and transport in various biological systems. LBP proteins are involved in the binding and transport of lipids, facilitating lipid homeostasis and cellular signaling processes. Their importance is underscored by their implications in numerous physiological and pathological conditions, including obesity, diabetes, cardiovascular diseases, and cancer. The ability to produce recombinant LBP proteins has transformed research methodologies, enabling detailed studies of their structure-function relationships and interactions with other biomolecules. Advances in recombinant DNA technology allow for the expression and purification of these proteins in significant quantities, making it possible to explore their therapeutic potentials. Understanding the mechanisms of LBP proteins at a molecular level not only contributes to basic science but also paves the way for developing novel therapeutic strategies targeting metabolic disorders. Consequently, the exploration of LBP recombinant proteins holds promise for providing insights into disease mechanisms and aiding in the discovery of targeted treatments in the context of lipid-related diseases.
