Analytical Data
-
Gene name
FGFR3
- Application
-
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
-
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.
Quality inspection process
Related Products
Protein Description
Fibroblast growth factor receptor 3 (FGFR3) is a member of the fibroblast growth factor receptor family, which plays a crucial role in various biological processes, including cell growth, differentiation, and bone development. Mutations in the FGFR3 gene have been linked to several skeletal disorders, most notably achondroplasia, the most common form of dwarfism. Research on FGFR3 recombinant proteins is essential for understanding its functional mechanisms, particularly how mutations affect receptor activity and downstream signaling pathways. By studying FGFR3 and its variants in a recombinant protein format, scientists can elucidate the structural and functional characteristics of the receptor, explore its role in disease pathogenesis, and identify potential therapeutic targets. Additionally, FGFR3 is involved in regulating cell proliferation and apoptosis, making it a significant focus in cancer research, particularly in tumors that express aberrant FGFR3 signaling. Developing FGFR3 recombinant proteins allows researchers to investigate the receptor’s interactions with ligands, assess its structural integrity, and evaluate the efficacy of potential inhibitors in combating FGFR3-related diseases. Overall, the study of FGFR3 recombinant proteins is integral to advancing our understanding of both genetic disorders and cancer biology, offering insights that could lead to novel treatment strategies.
