Cat: IPD-X23067

Recombinant Mouse Lumican/LUM Protein,His & Myc

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Analytical Data

  • Gene name

    Lumican/LUM

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Keratan sulfate proteoglycan lumican (KSPG lumican) (Lcn) (Ldc)

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P51885

  • Expression Region

    19-338aa

  • Molecular Weight

    44.0 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.

Quality inspection process

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Protein Description

Lumican, a member of the small leucine-rich proteoglycan family, plays a crucial role in extracellular matrix (ECM) organization and regulation of cell behavior. It is primarily expressed in connective tissues, including cartilage and corneal stroma, where it is involved in collagen fibril formation and maintenance of tissue integrity. Recent studies have highlighted Lumican's significance beyond structural functions; it is implicated in various pathological conditions, including cancer progression and fibrosis. The recombinant expression of Lumican (LUM) protein has garnered attention for its potential therapeutic applications, particularly in regenerative medicine. By producing LUM as a recombinant protein, researchers aim to investigate its specific interactions with cell surface receptors and ECM components, facilitating a deeper understanding of its biological roles. This has led to exploration of its use in improving wound healing, modulating inflammation, and even enhancing the efficacy of cancer treatments. Through advanced biotechnological methods, including gene cloning and protein purification, researchers are working to clarify Lumican’s multifaceted functions and optimize its application in clinical settings. The ongoing research is expected to provide insights into how manipulating Lumican levels could be harnessed for therapeutic strategies in various diseases, ultimately contributing to the development of novel treatments that leverage the regenerative properties of this important proteoglycan.

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