Cat: IPD-X20604

Recombinant Cynomolgus CD6 Protein(HEK293), Avi & His

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Analytical Data

  • Gene name

    CD6

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CD6 antigen; Cd6

  • Species

    Cynomolgus

  • Source

    HEK293

  • Tag

    C-Avi;C-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    XP_005577746

  • Expression Region

    H18-L399

  • Molecular Weight

    63-90 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

Langerin, also known as CD207, is a C-type lectin receptor predominantly expressed on Langerhans cells, a specialized subset of dendritic cells found in the epidermis. This receptor plays a critical role in the immune response by mediating the recognition and internalization of pathogens, such as viruses and bacteria, through its carbohydrate-binding activity. Due to its unique properties, Langerin is important for maintaining skin immune surveillance and tolerance. Research on recombinant Langerin/CD207 protein has gained importance for several reasons. First, understanding its structure and function can offer insights into the mechanisms of antigen presentation and T cell activation, crucial for developing novel immunotherapies. Additionally, Langerin's ability to bind to specific glycans makes it a potential target for vaccine development and targeted drug delivery systems. Studies involving recombinant Langerin also pave the way for exploring its role in various skin-related diseases, including infections, allergies, and autoimmune disorders. Furthermore, given the increasing interest in the interplay between the immune system and skin microbiota, Langerin's study may uncover new therapeutic avenues for maintaining skin health and combating dermal-related pathologies. Overall, ongoing research into Langerin/CD207 recombinant protein holds significant promise for advancing our understanding of immunology and therapeutic interventions in dermatological and systemic diseases.

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