Analytical Data
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基因名
FEN1
- Application
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别名
FEN1；RAD2;Flap endonuclease 1
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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
P39748
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表达区间
1-380aa
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氨基酸序列
MGIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGIGPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAAGKFKRGK
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分子量
50.0 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
FEN1 (Flap Endonuclease 1) is a vital enzyme involved in the DNA repair and replication processes, primarily responsible for removing RNA primers during DNA synthesis and processing Okazaki fragments on the lagging strand. The study of FEN1 has gained attention due to its critical role in maintaining genomic stability and its implications in various diseases, including cancer. Abnormal FEN1 activity has been linked to heightened susceptibility to malignancies, making it a potential target for therapeutic interventions. Understanding the structure and function of FEN1 is crucial for elucidating its mechanisms in DNA metabolism. Recent advances in recombinant protein technology have enabled the production of FEN1 in various systems, facilitating detailed biochemical and structural studies. Researchers aim to explore FEN1's catalytic mechanisms, substrate interactions, and regulatory pathways by employing techniques such as X-ray crystallography, circular dichroism, and kinetic assays. Insights gained from FEN1 research can contribute to the development of novel cancer therapies and enhance our understanding of DNA repair pathways, underscoring the enzyme's significance in molecular biology and medicine.
