Analytical Data
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Gene name
FGFR3
- Application
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Alternative Names
CD333; ACH; CEK2; JTK4; Achondroplasia; Thanatophoric Dwarfism
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Species
Human
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P22607
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Expression Region
397-806aa
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Molecular Weight
47.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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.
Quality inspection process
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Protein Description
Fibroblast growth factor receptor 3 (FGFR3) is a member of the fibroblast growth factor receptor family that plays a crucial role in bone development and maintenance. Mutations in the FGFR3 gene have been linked to several skeletal disorders, including achondroplasia, the most common form of skeletal dysplasia characterized by disproportionate short stature. The receptor functions as a tyrosine kinase, and its signaling pathways are involved in regulating cell proliferation, differentiation, and survival. Due to its significant role in growth plate regulation and the pathogenesis of various diseases, FGFR3 has emerged as an attractive target for therapeutic intervention. Research on recombinant FGFR3 proteins has enabled the exploration of its structural and functional properties, allowing for a better understanding of its signaling mechanisms in normal physiology and disease states. The use of recombinant technology facilitates the production of FGFR3 in a controlled environment, enabling detailed studies on its interaction with ligands and other cellular components. This research is critical for developing potential treatments that can modulate FGFR3 activity in conditions caused by its dysregulation. Additionally, studying FGFR3 interactions can contribute to the design of inhibitors that may alleviate symptoms of skeletal dysplasias, providing a pathway for innovative therapeutic strategies that can improve patient outcomes.
