Analytical Data
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基因名
dNER
- Application
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别名
dNER；BET；Delta and Notch-like epidermal growth factor-related receptor
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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
Q8NFT8
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表达区间
1-640aa
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氨基酸序列
MQPRRAQAPGAQLLPALALLLLLLGAGPRGSSLANPVPAAPLSAPGPCAAQPCRNGGVCTSRPEPDPQHPAPAGEPGYSCTCPAGISGANCQLVADPCASNPCHHGNCSSSSSSSSDGYLCICNEGYEGPNCEQALPSLPATGWTESMAPRQLQPVPATQEPDKILPRSQATVTLPTWQPKTGQKVVEMKWDQVEVIPDIACGNASSNSSAGGRLVSFEVPQNTSVKIRQDATASLILLWKVTATGFQQCSLIDGRSVTPLQASGGLVLLEEMLALGNNHFIGFVNDSVTKSIVALRLTLVVKVSTCVPGESHANDLECSGKGKCTTKPSEATFSCTCEEQYVGTFCEEYDACQRKPCQNNASCIDANEKQDGSNFTCVCLPGYTGELCQSKIDYCILDPCRNGATCISSLSGFTCQCPEGYFGSACEEKVDPCASSPCQNNGTCYVDGVHFTCNCSPGFTGPTCAQLIDFCALSPCAHGTCRSVGTSYKCLCDPGYHGLYCEEEYNECLSAPCLNAATCRDLVNGYECVCLAEYKGTHCELYKDPCANVSCLNGATCDSDGLNGTCICAPGFTGEECDIDINECDSNPCHHGGSCLDQPNGYNCHCPHGWVGANCEIHLQWKSGHMAESLTNMPRHSLY
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分子量
100 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
dNER (Drosophila Nucleotide Excision Repair) recombinant proteins are pivotal in the study of DNA repair mechanisms, particularly the nucleotide excision repair pathway, which is vital for maintaining genomic stability and preventing mutations. This pathway is responsible for the recognition and removal of a wide range of DNA lesions, including those caused by UV irradiation and chemical carcinogens. Understanding dNER proteins is essential, as they share significant functional similarities with human proteins involved in the same repair processes, offering insights into human genetic disorders resulting from defective DNA repair systems, such as xeroderma pigmentosum and cancer. Research on dNER recombinant proteins involves cloning, expression, and purification techniques to produce these proteins in model organisms like Drosophila. This allows scientists to study their interactions, enzymatic activities, and roles in the DNA repair process. Investigating these proteins also aids in elucidating the consequences of impaired nucleotide excision repair in organisms, serving as a model to better understand the underlying mechanisms in humans. By studying the structure-function relationships of dNER proteins, researchers aim to develop innovative therapeutic strategies to enhance DNA repair capabilities and mitigate the effects of DNA damage in various diseases. Thus, dNER recombinant protein research not only contributes to a foundational understanding of cellular defense mechanisms against DNA damage but also highlights its implications for health and disease management.
