Analytical Data
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基因名
NOC4L
- Application
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别名
NOC4L; Nucleolar complex protein 4 homolog; NOC4 protein homolog; NOC4-like protein; Nucleolar complex-associated protein 4-like protein
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9BVI4
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表达区间
1-516 aa
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氨基酸序列
MEREPGAAGVRRALGRRLEAVLASRSEANAVFDILAVLQSEDQEEIQEAVRTCSRLFGALLERGELFVGQLPSEEMVMTGSQGATRKYKVWMRHRYHSCCNRLGELLGHPSFQVKELALSALLKFVQLEGAHPLEKSKWEGNYLFPRELFKLVVGGLLSPEEDQSLLLSQFREYLDYDDTRYHTMQAAVDAVARVTGQHPEVPPAFWNNAFTLLSAVSLPRREPTVSSFYVKRAELWDTWKVAHLKEHRRVFQAMWLSFLKHKLPLSLYKKVLLIVHDAILPQLAQPTLMIDFLTRACDLGGALSLLALNGLFILIHKHNLEYPDFYRKLYGLLDPSVFHVKYRARFFHLADLFLSSSHLPAYLVAAFAKRLARLALTAPPEALLMVLPFICNLLRRHPACRVLVHRPHGPELDADPYDPGEEDPAQSRALESSLWELQALQRHYHPEVSKAASVINQALSMPEVSIAPLLELTAYEIFERDLKKKGPEPVPLEFIPAQGLLGRPGELCAQHFTLS
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分子量
84.9 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
NOC4L (Nucleolar Complex Related 4-Like) protein plays a crucial role in ribosome biogenesis and has been implicated in cellular stress responses, particularly in relation to the nucleolus, a subnuclear structure essential for ribosomal RNA synthesis and ribosome assembly. Research into NOC4L has gained momentum due to its association with various cellular processes, including gene expression regulation and cell cycle progression. Abnormalities in its function have been linked to several diseases, including cancer, highlighting the importance of understanding NOC4L's molecular mechanisms. Studies suggest that NOC4L may interact with other nucleolar proteins and ribonucleoprotein complexes, influencing their stability and function. Recent investigations aim to elucidate these interactions and their implications for ribosome production under both normal and stress conditions, providing insights into how cells adapt to environmental challenges. This research is not only vital for understanding fundamental cellular biology but also offers potential avenues for therapeutic interventions in diseases characterized by ribosomal dysfunction. As such, NOC4L continues to be a significant focus in molecular and cellular biology, with ongoing studies aimed at unraveling its complex role within the nucleolar framework and its impact on cellular homeostasis.
