Analytical Data
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基因名
FYN
- Application
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别名
FYN；Tyrosine-Protein kinase Fyn
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P06241
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表达区间
2-537aa
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氨基酸序列
GCVQCKDKEATKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYN NFHAAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDL SFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYF GKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVK HYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMP RLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTL KPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLL DFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNG LICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWS FGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIH CWKKDPEERPTFEYLQSFLEDYFTATEPQYQPGENL
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分子量
61 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.
