Cat: PA2000-761DB

Recombinant Human OSBP Protein,His

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Analytical Data

  • Gene name

    OSBP

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    OSBP;OSBP1;Oxysterol-binding Protein 1

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P22059

  • Expression Region

    324-407aa

  • AA Sequence

    GATVLPANTPGNVGSGKDQCCSGKGDMSDEDDENEFFDAPEIITMPENLG HKRTGSNISGASSDISLDEQYKHQLEETKKEKRT

  • Molecular Weight

    35 kDa

  • 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

OSBP (Oxysterol-Binding Protein) is a pivotal player in cellular lipid metabolism and signaling, functioning as a lipid sensor that interacts with oxysterols, a class of bioactive lipids derived from cholesterol. Research into OSBP has gained momentum due to its critical role in regulating the transport of lipids between cellular organelles, specifically the endoplasmic reticulum and the Golgi apparatus, thereby influencing various cellular processes including membrane biogenesis, cell proliferation, and apoptosis. OSBP also serves as an important mediator in the response to cellular stress and has been implicated in several pathological conditions, such as cardiovascular diseases and cancer, highlighting its potential as a therapeutic target. The study of OSBP recombinant proteins has provided valuable insights into its molecular mechanisms and interactions with other proteins and lipids. By elucidating the structural and functional aspects of OSBP, researchers aim to uncover the complexities of lipid metabolism and develop novel strategies for intervention in diseases associated with dysregulated lipid homeostasis. The development of recombinant OSBP proteins facilitates a better understanding of their biochemical properties, enabling the exploration of their role in cellular signaling pathways and overall lipid management within the cell. As such, the research on OSBP and its recombinant proteins is vital for advancing our understanding of lipid biology and its implications in health and disease.

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