Analytical Data
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基因名
SRSF10
- Application
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别名
40KDA SR-repressor protein ;SRrp40FUS-interacting serine-arginine-rich protein 1Splicing factor SRp38Splicing factor, arginine/serine-rich 13ATLS-associated protein with Ser-Arg repeats ;TASR ;TLS-associated protein with SR repeatsTLS-associated serine-arginine protein ;TLS-associated SR protein
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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-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O75494
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表达区间
1-183aa
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分子量
38.2 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
SRSF10, a member of the serine/arginine-rich splicing factor family, plays a critical role in pre-mRNA splicing and has been implicated in various cellular processes, including gene expression regulation, RNA metabolism, and cancer progression. Research into the recombinant SRSF10 protein is driven by its dual functions: as a splicing factor and a modulator of alternative splicing, which can influence the production of diverse protein isoforms essential for cellular functions. Notably, alterations in SRSF10 expression have been linked to several malignancies, underscoring its potential as a biomarker and therapeutic target. Furthermore, studies have shown that SRSF10 can interact with other proteins and RNA molecules, revealing its complex role in the splicing machinery. As researchers seek to unravel the mechanisms by which SRSF10 contributes to tumorigenesis and other diseases, the development of recombinant forms of the protein enables detailed analyses of its functional properties and interactions in vitro and in vivo. This research is crucial for understanding the broader implications of splicing regulation in health and disease, paving the way for innovative strategies in cancer therapy and other RNA-related disorders. Thus, SRSF10 serves as a compelling focal point for investigations aimed at elucidating the intricacies of gene regulation and RNA processing.
