Analytical Data
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基因名
APT
- Application
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别名
/
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种属
Escherichia coli O139:H28
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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
A7ZIM8
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表达区间
1-183aa
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分子量
27.3 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
The study of APT (Adenylate Phosphoryltransferase) recombinant proteins has gained considerable attention in recent years due to their pivotal role in various biological processes and potential therapeutic applications. APTs are essential enzymes involved in nucleotide metabolism, facilitating the transfer of phosphate groups, which is crucial for energy production and signal transduction in cells. With advances in biotechnology, scientists have been able to engineer recombinant APT proteins, allowing for a detailed examination of their structure-function relationships. This research not only enhances our understanding of enzymatic mechanisms but also paves the way for the development of novel drugs and diagnostic tools targeting diseases linked to metabolic dysregulation. Moreover, the ability to produce APTs in heterologous systems, such as bacteria or yeast, has made it possible to obtain these proteins in large quantities, facilitating biochemical assays and structural studies. By investigating the variations in recombinant APTs derived from different organisms, researchers aim to uncover evolutionary adaptations and optimize enzyme performance for industrial applications. Overall, the exploration of APT recombinant proteins holds significant promise for advancing both fundamental and applied sciences.












