Analytical Data
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基因名
FPG
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简介
FPG is a key base excision repair enzyme that recognizes and eliminates damaged bases, especially oxidized purines such as 8-oxoG. It acts on a variety of pathologies, including guanidinohydantoin: C, spiroiminodiahydantoin: C, thymine glycol: G, 5,6-dihydrouracil: G, and 5-hydroxy Uracil: G. FPG Protein, E.coli (His) is the recombinant E. coli-derived FPG protein, expressed by E. coli , with His tag. FPG Protein, E.coli (His), has molecular weight of ~30.3 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
MPELPEVETSRRGIEPHLVGATILHAVVRNGRLRWPVSEEIYRLSDQPVLSVQRRAKYLLLELPEGWIIIHLGMSGSLRILPEELPPEKHDHVDLVMSNGKVLRYTDPRRFGAWLWTKELEGHNVLTHLGPEPLSDDFNGEYLHQKCAKKKTAIKPWLMDNKLVVGVGNIYASESLFAAGIHPDRLASSLSLAECELLARVIKAVLLRSIEQGGTTLKDFLQSDGKPGYFAQELQVYGRKGEPCRVCGTPIVATKHAQRATFYCRQCQK
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分子量
30.3 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.
Quality inspection process
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Protein Description
FPG (Formamidopyrimidine-DNA glycosylase) is a pivotal enzyme involved in the base excision repair pathway, specifically targeting oxidative damage to DNA. Research on FPG recombinant proteins has gained prominence due to the increasing understanding of how oxidative stress contributes to various pathological conditions, including cancer, neurodegenerative diseases, and aging. FPG recognizes and excises damaged bases, particularly 7,8-dihydro-8-oxoguanine, which is a common product of oxidative DNA damage. This enzymatic activity not only ensures the integrity of genetic material but also plays a crucial role in preventing mutations that could lead to tumorigenesis. Given the significance of FPG in maintaining genomic stability, scientists have worked to produce recombinant forms of this protein for in-depth biochemical and structural studies. By engineering and expressing FPG in various host systems, researchers aim to elucidate its interaction with DNA substrates and other proteins involved in the DNA repair pathway. This research not only enhances the understanding of FPG's biological function but also paves the way for potential therapeutic applications, such as utilizing FPG as a target for drug development in cancers characterized by DNA repair deficiencies. Overall, the study of FPG recombinant proteins underscores the broader implications of DNA repair mechanisms in health and disease, providing insights that could lead to innovative strategies for disease intervention and prevention.
