Analytical Data
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Gene name
FGFR-3
- 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
E. coli
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Tag
N-His
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Purity
Greater than 97% as determined by reducing SDS-PAGE.
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Uniprot
P22607
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Expression Region
Val166~Gly377
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Molecular Weight
28kDa
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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
Related Products
Protein Description
Fibroblast growth factor receptor 3 (FGFR-3) is a transmembrane protein that plays a critical role in regulating cell growth, differentiation, and apoptosis, particularly in bone and cartilage development. Mutations in the FGFR3 gene are associated with various skeletal disorders, most notably achondroplasia, the most common form of disproportionate dwarfism. Research into FGFR-3 recombinant proteins is pivotal for understanding its biological functions and the mechanisms underlying FGFR-3-related diseases. By producing recombinant FGFR-3 proteins, scientists can investigate the signaling pathways affected by its mutations and explore potential therapeutic targets for conditions resulting from FGFR-3 dysregulation. These studies also facilitate the development of drugs that could modulate FGFR-3 activity, offering hope for novel treatments for skeletal dysplasias and other FGFR-3 related anomalies. Furthermore, the recombinant protein serves as a valuable tool for structure-function analyses, enabling the identification of crucial domains for ligand interaction and receptor activation. Overall, FGFR-3 recombinant protein research is at the forefront of both congenital disorder investigations and the broader field of targeted molecular therapies.
