Cat: IPD-X24512

Recombinant Human Galectin-8/LGALS8 Protein,GST

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Analytical Data

  • Gene name

    Galectin-8/LGALS8

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Po66 carbohydrate-binding protein

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O00214

  • Expression Region

    1-317aa

  • Molecular Weight

    62.8 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

Galectin-8 (LGALS8) is a member of the galectin family, a group of proteins characterized by their ability to bind beta-galactosides and play crucial roles in various biological processes, including cell adhesion, proliferation, and apoptosis. The study of LGALS8 has gained significant attention due to its involvement in critical physiological and pathological conditions, such as cancer, inflammation, and immune response regulation. Elevated levels of LGALS8 have been associated with tumor progression and metastasis, making it a potential biomarker and therapeutic target in oncology. Additionally, LGALS8 interacts with various cell surface glycoproteins and influences immune cell behavior, facilitating the understanding of its role in immune evasion by tumors. Given the importance of LGALS8 in such diverse biological functions, the production and characterization of recombinant LGALS8 protein are essential for studying its mechanisms of action and therapeutic potential. Advances in recombinant protein expression systems enable the generation of sufficient quantities of LGALS8 for detailed in vitro and in vivo studies, paving the way for novel therapeutic strategies targeting galectins in disease contexts. Research into LGALS8 not only enhances our understanding of its biological significance but also highlights its potential as a drug target and prognostic marker in various diseases.

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