Analytical Data
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Gene name
FGFR2
- Application
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Alternative Names
CD332; BEK; BFR1; CEK3; CFD1; ECT1; JWS; K-SAM; KGFR; TK14; Bacteria-Expressed Kinase,Keratinocyte Growth Factor Receptor; Craniofacial Dysostosis 1; Crouzon Syndrome
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by reducing SDS-PAGE.
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Uniprot
F1LSG7
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Expression Region
Arg41~Ala285
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Molecular Weight
34kDa
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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 2 (FGFR2) is a crucial member of the FGFR family, which plays significant roles in various biological processes including cell proliferation, differentiation, and tissue repair. Abnormalities in FGFR2 signaling have been implicated in several cancers, such as gastric and breast cancer, where mutations or overexpression contribute to tumorigenesis. Due to its pivotal role in cancer development, FGFR2 has emerged as a promising therapeutic target. The study of FGFR2 recombinant proteins is integral to understanding its function and the mechanisms underlying its involvement in oncogenic pathways. By producing FGFR2 in recombinant systems, researchers can obtain the protein in a controlled environment, allowing for detailed studies on its structure, binding affinity, and interactions with ligands and inhibitors. Furthermore, this research facilitates the development of targeted therapies, including monoclonal antibodies and small molecule inhibitors, aimed at disrupting aberrant FGFR2 signaling in cancer. Overall, the investigation of FGFR2 recombinant proteins not only enhances our understanding of receptor biology but also holds potential for advancing novel treatments for FGFR2-related malignancies.











