Cat: IPD-X20186

Recombinant Mouse L-selectin/CD62L Protein(HEK293), His

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Analytical Data

  • Gene name

    L-selectin/CD62L

  • 简介

    L-selectin, a calcium-dependent lectin, binds to glycoproteins on adjacent cells, facilitating lymphocyte attachment to endothelial cells in peripheral lymph nodes. This interaction is essential for leukocyte rolling along the endothelium and requires L-selectin's binding to SELPLG/PSGL1 and PODXL2, dependent on glycan and sulfation modifications. Sulfation of 'Tyr-51' on SELPLG is particularly important for L-selectin binding. L-selectin/CD62L Protein, Mouse (HEK293, His) is the recombinant mouse-derived L-selectin/CD62L protein, expressed by HEK293 , with C-His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Biological Activity

    Measured by the ability of the immobilized protein to support the adhesion of LS180 human colorectal adenocarcinoma cells. The ED50 for this effect is 5.230 μg/mL, corresponding to a specific activity is 191.205 units/mg. Measured by the ability of the immobilized protein to support the adhesion of LS180 human colorectal adenocarcinoma cells. The ED50 for this effect is 5.230 μg/mL, corresponding to a specific activity is 191.205 units/mg.

  • Alternative Names

    L-selectin; Sell; CD62 antigen-like family member L; LECAM1; CD62L; LAM-1

  • Species

    Mouse

  • Source

    HEK293

  • Tag

    C-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    NP_035476.1

  • Expression Region

    W39-N332

  • Protein Length

    Partial

  • Molecular Weight

    70-80 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

L-selectin, also known as CD62L, is a cell adhesion molecule primarily expressed on leukocytes, playing a critical role in the recruitment and homing of immune cells to sites of inflammation and lymphoid organs. Its function is mediated through interactions with specific carbohydrates expressed on endothelial cells and other cells, facilitating the rolling and adhesion of leukocytes during the inflammatory response. The study of L-selectin/CD62L recombinant proteins has garnered significant attention due to their potential applications in understanding immune system dynamics and developing therapeutic strategies for various diseases, including autoimmune disorders, allergies, and cancer. Researchers have focused on the structure-function relationship of L-selectin, investigating how its various domains contribute to its adhesion properties. Additionally, recombinant L-selectin proteins serve as valuable tools in experimental settings, allowing for the study of its interactions with ligands and the design of inhibitors that could modulate immune responses. The generation of these recombinant proteins has enabled detailed investigations into the mechanisms of leukocyte trafficking and has opened avenues for novel therapeutic interventions aimed at modulating immune cell behavior in different pathological contexts.


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