Analytical Data
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基因名
fum
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简介
Fum proteins crucially catalyze the interconversion of fumarate to L-malate in the tricarboxylic acid (TCA) cycle, maintaining metabolite flow in cellular energy metabolism. This critical step, if precisely regulated, helps generate energy and generates intermediates critical to cellular processes. fum Protein, Corynebacterium glutamicum (His) is the recombinant fum protein, expressed by E. coli , with N-6*His labeled tag.
- Application
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别名
fumC; Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase
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种属
Others
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表达系统
E. coli
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标签
N-6*His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q8NRN8
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表达区间
M1-F469
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蛋白长度
Partial
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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
FUM recombinant protein research focuses on the study and application of fumarate hydratase (FUM), an enzyme involved in the citric acid cycle, which plays a crucial role in cellular metabolism. This enzyme catalyzes the reversible hydration of fumarate to malate, and its dysfunction is associated with various metabolic disorders and certain cancers, particularly hereditary leiomyomatosis and renal cell cancer (HLRCC). Scientists are increasingly interested in FUM for its potential therapeutic applications, as understanding its structure and function can lead to novel treatments for such diseases. Advancements in genetic engineering and recombinant DNA technology have enabled the efficient production of FUM, allowing researchers to explore its enzymatic properties, optimize its activity for industrial applications, and develop inhibitors or activators for therapeutic interventions. Moreover, elucidating the molecular mechanisms underlying FUM function and its role in metabolic pathways can provide insights into tumorigenesis and metabolic regulation, promoting the development of targeted therapies. The growing body of literature on FUM underscores its significance in biochemistry and medicine, highlighting the potential for recombinant FUM in therapeutic applications and its importance in understanding complex metabolic processes.
