Cat: IPD-X24194

Recombinant Human WIF-1 Protein (HEK293),His

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Analytical Data

  • Gene name

    WIF-1

  • 简介

    WIF-1 protein critically binds to WNT protein, inhibits its activity and regulates the WNT signaling pathway. In addition to its inhibitory role, WIF-1 may also contribute to mesoderm segmentation, implicating its role in embryonic development. WIF-1 Protein, Human (HEK293, His) is the recombinant human-derived WIF-1 protein, expressed by HEK293 , with C-6*His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Biological Activity

    1.Measured by its ability to inhibit Wnt-3a-induced alkaline phosphatase production by MC3T3-E1 mouse preosteoblast cells. The ED50 this effect is 0.1022-0.1136 μg/mL in the presence of 20 ng/mL Recombinant Human Wnt-3a, corresponding to a specific activity is 8802.8169-9784.7358 units/mg. 2.Measured by its ability to inhibit Wnt-3a-induced alkaline phosphatase production by MC3T3-E1 mouse preosteoblast cells. The ED50 for this effect is ≤0.5 μg/mL in the presence of 10 ng/mL Recombinant Human Wnt-3a, corresponding to a specific activity is ≥2×103 U/mg. Measured by its ability to inhibit Wnt-3a-induced alkaline phosphatase production by MC3T3-E1 mouse preosteoblast cells. The ED50 for this effect is 0.1022 μg/mL in the presence of 20 ng/mL Recombinant Human Wnt-3a, corresponding to a specific activity is 9784.7358 units/mg.

  • Alternative Names

    Wnt Inhibitory Factor 1; WIF-1; WIF1

  • Species

    Human

  • Source

    HEK293

  • Tag

    C-6*His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    AAH18037.1

  • Expression Region

    G29-W379

  • AA Sequence

    GPPQEESLYLWIDAHQARVLIGFEEDILIVSEGKMAPFTHDFRKAQQRMPAIPVNIHSMNFTWQAAGQAEYFYEFLSLRSLDKGIMADPTVNVPLLGTVPHKASVVQVGFPCLGKQDGVAAFEVDVIVMNSEGNTILKTPQNAIFFKTCQQAECPGGCRNGGFCNERRICECPDGFHGPHCEKALCTPRCMNGGLCVTPGFCICPPGFYGVNCDKANCSTTCFNGGTCFYPGKCICPPGLEGEQCEISKCPQPCRNGGKCIGKSKCKCSKGYQGDLCSKPVCEPGCGAHGTCHEPNKCQCQEGWHGRHCNKRYEASLIHALRPAGAQLRQHTPSLKKAEERRDPPESNYIW

  • Protein Length

    Partial

  • Molecular Weight

    42-48 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

WIF-1 (Wnt Inhibitory Factor-1) is a secreted protein that plays a critical role in the regulation of the Wnt signaling pathway, which is essential for various developmental processes and cell proliferation. Abnormal activation of Wnt signaling is associated with multiple cancers, making WIF-1 an important molecule for potential therapeutic applications. Research has highlighted that WIF-1 can antagonize Wnt signaling by binding to Wnt ligands, thereby preventing their interaction with Frizzled receptors. Understanding the structure and function of WIF-1 has significant implications for targeted cancer therapies and regenerative medicine, as it may provide insights into mechanisms of tumor suppression and tissue repair. Recent studies have focused on the recombinant expression of WIF-1 to establish its functional characteristics and properties. This involves leveraging advanced molecular biology techniques to produce WIF-1 in host systems, allowing for detailed biochemical analyses and the exploration of its therapeutic potential. Ongoing research also aims to elucidate the role of WIF-1 in various biological contexts, including its implications in embryonic development and tissue homeostasis. As a candidate for biomarker development and a target for therapeutic intervention, WIF-1 continues to be an area of intense study, with the hope of translating these findings into clinical applications for cancer treatment and regenerative medicine.

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