Analytical Data
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Gene name
FGFR-2
- 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
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P21802
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Expression Region
Thr157~Glu377
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Molecular Weight
32kDa
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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 2 (FGFR-2) is a vital member of the FGFR family, known for its critical roles in cell proliferation, differentiation, and survival. It is particularly implicated in various physiological processes, including angiogenesis and wound healing. Dysregulation or mutations in FGFR-2 are associated with several diseases, including certain cancers and congenital disorders such as Apert syndrome. The study of FGFR-2 has gained prominence due to its potential as a therapeutic target. Researchers have been focusing on developing recombinant FGFR-2 proteins to understand its structure-function relationships and the mechanisms underlying its activation. Such recombinant proteins can be used in a variety of applications, such as drug screening, the development of targeted therapies, and investigating FGFR-2's role in cell signaling pathways. Furthermore, the generation of FGFR-2 variants and their interactions with specific ligands can provide insights into the receptor's ligand-binding dynamics and subsequent downstream signaling effects. As FGFR-2 continues to be a focal point in cancer biology and regenerative medicine, the development and characterization of its recombinant proteins could lead to novel therapeutic strategies that exploit this receptor's essential functions.
