Analytical Data
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Gene name
FYN
- Application
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Alternative Names
FYN；Tyrosine-Protein kinase Fyn
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
2-537aa
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AA Sequence
GCVQCKDKEATKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYN NFHAAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDL SFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYF GKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVK HYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMP RLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTL KPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLL DFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNG LICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWS FGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIH CWKKDPEERPTFEYLQSFLEDYFTATEPQYQPGENL
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Molecular Weight
61 kDa
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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 critical member of the Src family of tyrosine kinases, playing a pivotal role in various cellular processes such as signaling pathways, cell growth, differentiation, and survival. Its involvement in the immune response, especially in T-cell signaling, has made it a significant focus of research, particularly due to its implications in diseases like cancer and autoimmune disorders. The restructuring of FYN into a recombinant protein form has opened up new avenues for scientific investigation, allowing for a better understanding of its biochemical properties and interactions. This recombinant version enables researchers to study the structure-function relationships of FYN in controlled conditions, elucidating its mechanisms of action at a molecular level. Moreover, exploring FYN as a therapeutic target has gained traction, as its deregulation is associated with various pathologies. The development and characterization of FYN recombinant proteins facilitate high-throughput screening for potential inhibitors, paving the way for novel therapeutic strategies. Hence, the study of FYN recombinant proteins not only enhances our understanding of fundamental biological processes but also holds promise for innovative treatments in diseases driven by aberrant FYN activity.
