Cat: IPD-X29432

Recombinant Human LSR Protein,His & GST

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Analytical Data

  • Gene name

    LSR

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    LISCH7; ILDR3; LISCH; Lipolysis-Stimulated Remnant; Immunoglobulin-Like Domain Containing Receptor 3

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His & GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q86X29

  • Expression Region

    Lys335~Arg589

  • Molecular Weight

    68kDa

  • 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

LSR (Lipid Storage Regulator) is a protein that plays a crucial role in lipid metabolism and homeostasis, making it a significant subject of study in the fields of bioenergetics and cell biology. Research has shown that LSR is involved in the regulation of lipid droplets, which are essential for storing fats and providing energy to cells. Dysregulation of lipid storage and metabolism is linked to a variety of metabolic disorders, including obesity, diabetes, and cardiovascular diseases. Understanding the mechanisms by which LSR functions could provide insights into these conditions and highlight potential therapeutic targets. Recent advancements in recombinant protein technology have enabled the production and characterization of LSR, facilitating in-depth studies of its structure, function, and interactions with other cellular components. By leveraging techniques such as molecular cloning, protein expression systems, and biochemical assays, researchers aim to elucidate the detailed role of LSR in lipid metabolism. Furthermore, the study of LSR’s recombinant protein offers the opportunity to explore its potential applications in metabolic engineering and the development of novel strategies for treating metabolic diseases. Overall, the investigation of LSR as a recombinant protein not only enhances our understanding of lipid biology but also paves the way for innovative approaches to manage and prevent metabolic disorders.

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