Analytical Data
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基因名
SFRS12
- Application
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别名
SREK1; SFRS12; SRRP86Splicing regulatory glutamine/lysine-rich protein 1; Serine/arginine-rich-splicing regulatory protein 86; SRrp86; Splicing factor; arginine/serine-rich 12; Splicing regulatory protein 508; SRrp508
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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
Q8WXA9
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表达区间
421-508 aa
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氨基酸序列
KERDHISERRERERSTSMRKSSNDRDGKEKLEKNSTSLKEKEHNKEPDSSVSKEVDDKDAPRTEENKIQHNGNCQLNEENLSTKTEAV
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分子量
17.3 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
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Protein Description
SFRS12, or splicing factor, arginine/serine-rich 12, is a crucial protein involved in the regulation of pre-mRNA splicing. It belongs to the serine/arginine-rich (SR) protein family, which plays a significant role in the maturation of mRNA and the overall regulation of gene expression. The study of SFRS12 has gained attention due to its association with various cellular processes, including cell growth, differentiation, and the response to stress. Recent research has highlighted its potential role in cancer biology, as alterations in splicing factors can lead to aberrant gene expression and contribute to tumorigenesis. Moreover, SFRS12 has been implicated in various diseases beyond cancer, such as neurodegenerative disorders and developmental syndromes. Understanding the structure and function of SFRS12, as well as its interaction with other splicing factors and RNA, is essential for elucidating its mechanisms in normal and pathological conditions. Investigating SFRS12's role in these contexts could provide insights into therapeutic targets for diseases linked to splicing dysregulation, highlighting the protein's significance in molecular biology and medicine.












