Cat: IPD-X38151

Recombinant Human FGFR-3 Protein (HEK293),Fc

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Analytical Data

  • Gene name

    FGFR-3

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Fibroblast growth factor receptor 3; FGFR-3; CD333; FGFR3; JTK4; IIIc

  • Species

    Human

  • Source

    HEK293

  • Tag

    C- Fc

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P22607

  • Expression Region

    23-375aa

  • Molecular Weight

    64.8 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

FGFR3 (Fibroblast Growth Factor Receptor 3) is a receptor tyrosine kinase that plays a crucial role in bone development and growth regulation. Mutations in the FGFR3 gene are associated with a variety of skeletal dysplasias, most notably achondroplasia, which is the most common form of human dwarfism. The study of FGFR3 recombinant proteins is essential for understanding the molecular mechanisms underlying these conditions and for developing potential therapeutic interventions. Researchers have focused on producing FGFR3 as a recombinant protein to investigate its structure-function relationships, signaling pathways, and interactions with other molecules. This recombinant protein serves as a valuable tool for elucidating the effects of specific mutations and for screening small molecules or biologics that can modulate FGFR3 activity. Given the receptor's involvement in both normal and pathological bone growth, FGFR3 recombinant protein research holds promise not only for enhancing our understanding of skeletal disorders but also for advancing drug development efforts aimed at correcting the dysregulated signaling pathways associated with FGFR3 mutations. Furthermore, these studies can pave the way for targeted therapies that could improve treatment outcomes for patients with FGFR3-related disorders. Overall, FGFR3 recombinant protein research is significant for both basic science and clinical applications, highlighting the intricate connections between genetics, protein function, and disease management.

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