Cat: IPD-X39085

Recombinant Human OSBPL8 Protein,His

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Analytical Data

  • Gene name

    OSBPL8

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ORP8; OSBP10; Oxysterol-Binding Protein-Related Protein 8

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9BZF1

  • Expression Region

    Val148~Lys265

  • Molecular Weight

    15kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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.

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Protein Description

OSBPL8, a member of the oxysterol-binding protein (OSBP) family, is involved in lipid metabolism and cellular signaling. Research on OSBPL8 has gained traction due to its potential implications in various biological processes, including cholesterol transport, lipid synthesis, and the regulation of metabolic pathways. The protein has been shown to interact with multiple organelles, such as the endoplasmic reticulum and lipid droplets, highlighting its role in maintaining cellular lipid homeostasis. Dysregulation of OSBPL8 has been linked to several diseases, including metabolic disorders and cancer, making it a target of interest for therapeutic interventions. Understanding the structure and function of OSBPL8, particularly its interactions with different lipids and cellular components, is essential for unraveling its role in disease context and could inform the development of novel strategies for treatment. Researchers are exploring the potential of OSBPL8 as a biomarker for disease diagnosis and progression, as well as its utility in drug delivery systems. As the field progresses, the focus is not only on elucidating the basic biology of OSBPL8 but also on its translational potential in clinical applications. This makes OSBPL8 a significant subject of study in both fundamental and applied biomedical research.

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