Analytical Data
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Gene name
OSBP
- Application
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Alternative Names
OSBP1
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Species
Human
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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
P22059
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Expression Region
Thr546~Phe807
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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 OSBP (Oxysterol-Binding Protein) and its recombinant proteins has garnered significant attention due to the critical roles these proteins play in cellular lipid metabolism and signaling. OSBP is a key player in the transport of sterols and other lipids between cellular organelles, particularly between the endoplasmic reticulum and the Golgi apparatus. The ability of OSBP to bind oxysterols, which are oxidized derivatives of cholesterol, connects it to various physiological processes, including cholesterol homeostasis, membrane dynamics, and the regulation of cholesterol and lipid levels in cells. Dysregulation of OSBP is implicated in several diseases, including metabolic disorders, neurodegenerative diseases, and cancer. Thus, investigating OSBP and its variants through recombinant protein techniques allows for a deeper understanding of its structure-function relationships, interaction with lipid molecules, and its role in cellular pathways. Furthermore, the use of recombinant OSBP provides valuable insights into potential therapeutic targets, as modulating its function could influence lipid-related diseases. Research involving the characterization of OSBP's binding properties, structural studies, and functional assays is essential for developing novel strategies in lipid management and disease treatment, making it a prominent focus in molecular biology and biomedicine.
