Analytical Data
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基因名
UDG
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简介
UDG Protein, an uracil-DNA glycosylase, plays a pivotal role in DNA repair by excising uracil residues, addressing misincorporation or deamination-induced uracil. This activity is crucial for genomic integrity, preventing mutagenesis. UDG's precision in recognizing and excising uracil underscores its significance in cellular DNA repair mechanisms and fidelity. UDG Protein, E.coli (His) is the recombinant E. coli-derived UDG protein, expressed by E. coli , with His labeled tag. UDG Protein, E.coli (His), has molecular weight of ~25.7 kDa.
- Application
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种属
E.coli
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表达系统
E. coli
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标签
His
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纯度
Greater than 90% as determined by SDS-PAGE.
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氨基酸序列
MANELTWHDVLAEEKQQPYFLNTLQTVASERQSGVTIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVRPGIAIPPSLLNMYKELENTIPGFTRPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGSHAQKKGAIIDKQRHHVLKAPHPSPLSAHRGFFGCNHFVLANQWLEQRGETPIDWMPVLPAESE
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分子量
25.7 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
UDG (Uracil-DNA Glycosylase) is an enzyme that plays a crucial role in the base excision repair pathway, specifically in the recognition and removal of uracil from DNA. This process is essential for maintaining genomic stability, as uracil can arise from the deamination of cytosine or be incorporated into DNA during replication. Impairments in UDG function have been implicated in various diseases, including cancer, making it an important target for therapeutic interventions. Researchers have been investigating the structure and function of UDG to understand its mechanism of action at the molecular level. The recombinant expression of UDG has facilitated detailed studies on its enzymatic properties, substrate specificity, and interaction with DNA. Furthermore, UDG's potential applications in biotechnology, such as its use in gene editing and synthetic biology, have spurred interest in optimizing its activity and stability. As studies continue to reveal the complexities of UDG's role in DNA repair and its broader biological implications, it remains a significant focus of research aimed at developing novel strategies for disease treatment and prevention.
