Analytical Data
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基因名
DPYD
- Application
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别名
DPYD;Dihydropyrimidine dehydrogenase [NADP(+)]
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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
Q12882
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表达区间
1-173aa
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氨基酸序列
MAPVLSKDSADIESILALNPRTQTHATLCSTSAKKLDKKHWKRNPDKNCF NCEKLENNFDDIKHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSF ITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCNLYATEEGPI NIGGLQQFATETLILAFSLMNHL
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分子量
45 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
Dihydropyrimidine dehydrogenase (DPYD) is a pivotal enzyme in the pyrimidine catabolic pathway, primarily responsible for the degradation of the nucleobases uracil and thymine. Deficiencies in DPYD can lead to severe adverse drug reactions, particularly in patients receiving fluoropyrimidine-based chemotherapies, such as 5-fluorouracil (5-FU), used in treating various cancers. Genetic polymorphisms in the DPYD gene significantly influence enzyme activity, leading to variability in drug metabolism and patient response. Consequently, the study of DPYD recombinant proteins has garnered significant attention, as it allows researchers to investigate the enzyme's structure-function relationships, characterize its kinetic properties, and explore potential inhibitors or activators that could modulate its activity. Understanding these aspects is crucial for developing personalized medicine approaches, optimizing chemotherapy regimens, and minimizing toxicities associated with pyrimidine analogs. Furthermore, DPYD research contributes to the broader field of pharmacogenomics, elucidating how genetic variations affect individual responses to drugs, thereby enhancing therapeutic efficacy and safety.












