Cat: IPD-X20552

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 90% 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 is a member of the sialic acid-binding immunoglobulin-like lectins (Siglecs) family, which play crucial roles in cell signaling and immune regulation. Research has shown that Siglec-5 is predominantly expressed on immune cells, such as monocytes and macrophages, and is involved in modulating immune responses, particularly in the context of inflammation and pathogen recognition. Understanding the function and mechanisms of Siglec-5 is critical for elucidating its role in various immunological disorders, including autoimmune diseases and infections. Recent studies have indicated that Siglec-5 can interact with sialylated glycoproteins, affecting cellular communication and immune evasion strategies employed by pathogens. Furthermore, the development of recombinant Siglec-5 proteins allows for in-depth exploration of its biological activity and could aid in the development of novel therapeutic strategies aimed at targeting specific immune pathways. Enhanced knowledge of Siglec-5 interactions and signaling pathways may reveal potential implications for treating diseases characterized by immune dysregulation. Overall, ongoing research involving Siglec-5 recombinant proteins is pivotal for advancing our understanding of immune regulation and discovering new avenues for clinical interventions.

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