Analytical Data
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Gene name
FYN
- Application
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Alternative Names
SLK; SYN; c-Fyn; Src-like kinase
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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 90% as determined by SDS-PAGE.
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Uniprot
P06241
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Expression Region
Gly2~Leu537
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Molecular Weight
64kDa
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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
FYN is a member of the Src family of protein tyrosine kinases, which play a vital role in various cellular processes such as proliferation, differentiation, and survival. Dysregulation of FYN has been implicated in several diseases, including cancers and neurodegenerative disorders. Research on FYN has intensified due to its potential as a therapeutic target; however, the complex regulatory mechanisms and its interaction with other signaling pathways remain poorly understood. The study of FYN recombinant proteins has emerged as a promising approach to elucidate its structure-function relationships and to explore its contributions to cellular signaling networks. By generating and analyzing FYN reconstituted in vitro, researchers aim to gain insights into its kinase activity, substrate specificity, and regulatory mechanisms. This understanding could pave the way for the development of novel therapeutic strategies aimed at modulating FYN activity in pathological conditions, contributing to advancements in both cancer treatment and neurobiology. The application of recombinant technology in FYN research holds the potential to revolutionize our understanding of protein tyrosine kinases and their roles in human health and disease.
