关键信息
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基因名
NOL4
- 应用
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别名
NOL4; NOLP; HRIHFB2255Nucleolar protein 4; Nucleolar-localized protein
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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
O94818
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表达区间
1-638 aa
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氨基酸序列
MESERDMYRQ FQDWCLRTYG DSGKTKTVTR KKYERIVQLL NGSESSSTDN AKFKFWVKSK GFQLGQPDEV RGGGGGAKQV LYVPVKTTDG VGVDEKLSLR RVAVVEDFFD IIYSMHVETG PNGEQIRKHA GQKRTYKAIS ESYAFLPREA VTRFLMSCSE CQKRMHLNPD GTDHKDNGKP PTLVTSMIDY NMPITMAYMK HMKLQLLNSQ QDEDESSIES DEFDMSDSTR MSAVNSDLSS NLEERMQSPQ NLHGQQDDDS AAESFNGNET LGHSSIASGG THSREMGDSN SDGKTGLEQD EQPLNLSDSP LSAQLTSEYR IDDHNSNGKN KYKNLLISDL KMEREARENG SKSPAHSYSS YDSGKNESVD RGAEDLSLNR GDEDEDDHED HDDSEKVNET DGVEAERLKA FNMFVRLFVD ENLDRMVPIS KQPKEKIQAI IDSCRRQFPE YQERARKRIR TYLKSCRRMK RSGFEMSRPI PSHLTSAVAE SILASACESE SRNAAKRMRL ERQQDESAPA DKQCKPEATQ ATYSTSAVPG SQDVLYINGN GTYSYHSYRG LGGGLLNLND ASSSGPTDLS MKRQLATSSG SSSSSNSRPQ LSPTEINAVR QLVAGYRESA AFLLRSADEL ENLILQQN
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分子量
71.3 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.
质检流程
相关产品
背景信息
NOL4, a nucleolar protein, has gained attention in recent years due to its potential role in cellular processes such as ribosome biogenesis, RNA metabolism, and stress response. This protein is part of the nucleolar structure, which is critical for the assembly of ribosomal RNA and proteins into ribosomes, essential for protein synthesis in all living cells. Abnormalities in NOL4 expression levels have been linked to various diseases, including cancer, highlighting its importance in cellular homeostasis and pathology. Studies have demonstrated that NOL4 interacts with several key proteins involved in cell cycle regulation and apoptosis, suggesting that it may serve as a crucial regulator in these processes. Furthermore, recent advancements in recombinant protein technology have facilitated the production and purification of NOL4, allowing researchers to investigate its structure-function relationships and mechanisms of action in detail. Understanding the precise roles of NOL4 in cellular functions could provide insights into its potential as a therapeutic target and biomarker in disease contexts. Consequently, ongoing research focuses on elucidating the molecular interactions of NOL4 and its implications in health and disease, paving the way for novel strategies in medical intervention.
