Cat: IPD-X14444

Recombinant Human FGFR-4 Protein , His

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Analytical Data

  • Gene name

    FGFR-4

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CD334; JTK2; TKF

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by reducing SDS-PAGE.

  • Uniprot

    P22455

  • Expression Region

    Val168~Asp369

  • Molecular Weight

    27kDa

  • 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

Fibroblast Growth Factor Receptor 4 (FGFR4) is a member of the fibroblast growth factor receptor family, which plays a crucial role in various biological processes, including cell growth, differentiation, and metabolism. FGFR4 is particularly associated with the progression of several types of cancers, such as hepatocellular carcinoma and prostate cancer, where its overexpression correlates with poor prognosis. Given its significant role in tumorigenesis, FGFR4 has emerged as a potential therapeutic target, driving research into the development of FGFR4-specific inhibitors and therapies. The study of FGFR4 recombinant proteins is vital for understanding its structure-function relationships and interactions with ligands, which can inform the design of selective inhibitors. Furthermore, recombinant FGFR4 proteins facilitate the investigation of downstream signaling pathways, such as the MAPK and PI3K/Akt pathways, that are activated upon FGFR4 engagement. Advances in biotechnological methods have enabled the production of these proteins in various systems, allowing researchers to conduct detailed functional assays and structural analyses. Overall, the characterization of FGFR4 recombinant proteins is a foundational step in developing targeted therapeutics aimed at treating FGFR4-driven malignancies and improving clinical outcomes for patients.

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