Analytical Data
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基因名
SNRPC
- Application
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别名
SNRP-C
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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
P09234
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表达区间
Pro2~Arg159
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分子量
21kDa
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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
SNRPC, or the Small Nuclear Ribonucleoprotein Polypeptide C, is a crucial component of the spliceosome, the complex responsible for pre-mRNA splicing in eukaryotic cells. Research into SNRPC has gained momentum due to its significant role in gene expression regulation and potential implications in various diseases. Dysregulation of splicing processes can lead to the development of cancers, neurodegenerative disorders, and other genetic conditions. Understanding the structure and function of SNRPC is essential for elucidating how splicing machinery operates and how mutations might disrupt these processes. Recent studies have focused on characterizing SNRPC's interactions with RNA and other spliceosome components, utilizing techniques such as cryo-electron microscopy and mass spectrometry to reveal its functional dynamics. Additionally, the potential for SNRPC to serve as a therapeutic target in diseases associated with splicing anomalies has emerged, prompting investigations into small molecules that could modify its activity. Overall, the research surrounding SNRPC is pivotal not only for basic biological understanding but also for exploring innovative strategies in disease treatment and prevention.
