Analytical Data
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基因名
FYN
- Application
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别名
SLK; SYN; c-Fyn; Src-like kinase
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种属
Human
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表达系统
E. coli
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标签
N-His
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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
Gly2~Leu537
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分子量
64kDa
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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
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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.
