Analytical Data
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基因名
UGPA
- Application
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别名
(UDP-glucose pyrophosphorylase)(UDPGP)(UGPase)
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种属
Musa acuminata
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9SDX3
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表达区间
1-467aa
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分子量
58.8 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
UGPA (UDP-glucose pyrophosphorylase) is an enzyme that plays a crucial role in the synthesis of activated glucose, specifically UDP-glucose, which is a key precursor in various metabolic pathways, including glycosylation and polysaccharide biosynthesis. The study of UGPA is particularly significant due to its potential applications in biotechnology and medicine, where manipulating glycosylation processes can lead to enhanced production of therapeutic glycoproteins and improved vaccine efficacy. Understanding the structure and function of UGPA can provide insights into its regulatory mechanisms and its interaction with other metabolic enzymes. Recent advancements in molecular biology techniques and structural genomics have enabled researchers to explore the enzymatic mechanisms of UGPA at the atomic level, paving the way for the development of engineered variants with improved activity or altered substrate specificity. Additionally, the exploration of UGPA's role across different organisms highlights its evolutionary significance and potential for biotechnological exploitation across various fields, such as agriculture, where increasing resistance to pathogens through glycan modifications can be valuable. Overall, the comprehensive study of UGPA and its recombinant forms is vital in both fundamental and applied research, opening new avenues for innovation in glycan engineering and metabolic engineering.












