Cat: IPD-X22820

Recombinant Mouse Ficolin-1 Protein,His

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Analytical Data

  • Gene name

    Ficolin-1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (Collagen/fibrinogen domain-containing protein 1)(Ficolin-A)(Ficolin-alpha)(M-ficolin)

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O70165

  • Expression Region

    18-334aa

  • Molecular Weight

    38.5 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

Ficolin-1, also known as elictin, is a pattern recognition receptor that plays a crucial role in the innate immune system. It is primarily produced in the liver and released into the bloodstream, where it participates in the recognition of pathogen-associated molecular patterns (PAMPs) such as bacterial components and certain viruses. The significance of Ficolin-1 lies in its ability to mediate opsonization, enhance phagocytosis, and activate the complement system, thereby contributing to the host's defense against infections. Studies have shown that Ficolin-1 also plays a role in various diseases, including autoimmune disorders and cancer, making it a potential biomarker for disease diagnosis and progression. The recombinant form of Ficolin-1 has gained attention in research, as it offers a valuable tool for studying its biological functions and therapeutic applications. Scientists are exploring its structural properties, interaction with pathogens, and mechanisms of action in immune responses. Additionally, the recombinant protein could be leveraged for developing novel immunotherapeutic strategies aimed at enhancing immune responses or modulating inflammation. Understanding Ficolin-1's role in immunity at a molecular level could pave the way for innovative approaches to treat infectious diseases and autoimmune conditions. Overall, the recombinant study of Ficolin-1 holds promise for expanding our knowledge of innate immunity and developing therapeutic applications to harness or modulate immune functions effectively.

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