Analytical Data
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基因名
UPRT
- Application
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别名
FUR1
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种属
Human
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表达系统
E. coli
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标签
N- His & GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q96BW1
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表达区间
Asn75~Ala297
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分子量
55kDa
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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
Related Products
Protein Description
The study of UPRT (Uracil Phosphoribosyltransferase) recombinant protein has gained significant interest due to its potential applications in biotechnology and medicine. UPRT plays a crucial role in the pyrimidine salvage pathway, facilitating the conversion of uracil to UMP (uridine monophosphate), which is vital for nucleic acid synthesis and cellular metabolism. Given its function, UPRT is considered an attractive target for drug development, particularly in the context of treating parasitic infections and cancer, where it can be exploited to enhance the efficacy of antimetabolite therapies. Recombinant UPRT, produced through genetic engineering techniques, allows for the detailed study of its enzymatic properties, structural characteristics, and interactions with various inhibitors. This research not only provides insights into its biological significance but also paves the way for designing novel therapeutic strategies. Moreover, the ability to produce UPRT in a controlled environment enhances the prospects for high-throughput screening of chemical libraries aimed at identifying new drug candidates. Overall, the exploration of UPRT recombinant protein is crucial for advancing our understanding of its biological roles and the potential to manipulate its function for therapeutic benefits.
