Cat: IPD-X35856

Recombinant Human Siglec-5 Protein (HEK293),hFc

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Analytical Data

  • Gene name

    Siglec-5

  • 简介

    Siglec-5 Protein, a putative adhesion molecule, participates in sialic-acid dependent cellular binding, showing equal affinity for alpha-2,3-linked and alpha-2,6-linked sialic acid. Its sialic acid recognition site may be masked through cis interactions with sialic acids on the same cell surface. Siglec-5 Protein, Human (HEK293, Fc) is the recombinant human-derived Siglec-5 protein, expressed by HEK293 , with C-hFc labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Biological Activity

    Measured by its binding ability in a functional ELISA. Immobilized Siglec-5 at 1 μg/mL (100 μL/well) can bind Anti Siglec-5 antibody. The ED50 for this effect is 0.7241 μg/mL. Measured by its binding ability in a functional ELISA. Immobilized Siglec-5 at 1 μg/mL (100 μL/well) can bind Anti Siglec-5 antibody. The ED50 for this effect is 0.7241 μg/mL.

  • Alternative Names

    Sialic acid-binding Ig-like lectin 5; Siglec-5; CD33 antigen-like 2; Obesity-binding protein 2; OB-BP2; CD170

  • Species

    Human

  • Source

    HEK293

  • Tag

    C-hFc

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    O15389

  • Expression Region

    E17-T434

  • AA Sequence

    EKPVYELQVQKSVTVQEGLCVLVPCSFSYPWRSWYSSPPLYVYWFRDGEIPYYAEVVATNNPDRRVKPETQGRFRLLGDVQKKNCSLSIGDARMEDTGSYFFRVERGRDVKYSYQQNKLNLEVTALIEKPDIHFLEPLESGRPTRLSCSLPGSCEAGPPLTFSWTGNALSPLDPETTRSSELTLTPRPEDHGTNLTCQMKRQGAQVTTERTVQLNVSYAPQTITIFRNGIALEILQNTSYLPVLEGQALRLLCDAPSNPPAHLSWFQGSPALNATPISNTGILELRRVRSAEEGGFTCRAQHPLGFLQIFLNLSVYSLPQLLGPSCSWEAEGLHCRCSFRARPAPSLCWRLEEKPLEGNSSQGSFKVNSSSAGPWANSSLILHGGLSSDLKVSCKAWNIYGSQSGSVLLLQGRSNLGT

  • Protein Length

    Partial

  • Molecular Weight

    90-120 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

Siglec-5, a member of the SIGLEC (Sialic Acid Binding Ig-like Lectin) family, plays a crucial role in the immune system by modulating the activity of immune cells through its interaction with sialic acid, a common carbohydrate found on the surface of many cells. Research has indicated that Siglec-5 is primarily expressed on immune cells such as macrophages and dendritic cells, where it functions as an inhibitory receptor, dampening the immune response and thus contributing to the maintenance of immune tolerance. Its implications in various diseases, including autoimmune disorders and infections, have garnered significant attention in immunology. Studies have focused on the potential of Siglec-5 as a therapeutic target, investigating how modulation of its activity could enhance anti-tumor immunity or improve responses to vaccines. The engineering of Siglec-5 recombinant proteins has emerged as a promising avenue for understanding its biological functions and developing novel immunotherapeutic strategies. By producing these recombinant proteins, researchers aim to dissect the molecular mechanisms underlying Siglec-5's immunological roles and explore its potential utility in clinical applications, particularly in controlling inflammatory diseases and enhancing immune responses. Overall, the study of Siglec-5 and its recombinant forms represents a significant step towards harnessing the body's innate immune functions in the fight against diseases.

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