Analytical Data
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基因名
purF
- Application
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别名
(ATase(Glutamine phosphoribosylpyrophosphate amidotransferase)(GPATase)
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种属
Mycobacterium tuberculosis
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表达系统
E. coli
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P9WHQ6
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表达区间
35-527aa
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分子量
56.5 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 purF gene encodes an enzyme involved in the de novo synthesis pathway of purine nucleotides, which are essential for various cellular functions, including DNA and RNA synthesis, energy metabolism, and cell signaling. Research on purF recombinant protein has garnered attention due to its role in regulating purine metabolism and its potential implications in understanding certain diseases, such as cancer and metabolic disorders. Recombinant purF protein is instrumental for studying the enzyme's structure, function, and interactions, allowing scientists to elucidate the mechanisms that govern purine biosynthesis. Moreover, by producing purF in a heterologous system, researchers can investigate its enzymatic properties, explore its potential as a therapeutic target, and develop inhibitors that could selectively modulate purine metabolism. This research is also crucial for synthetic biology applications, where purF can be utilized to engineer metabolic pathways in microorganisms for bioproduction of nucleotides or pharmaceuticals. Overall, the exploration of purF recombinant protein is pivotal for advancing our understanding of cellular metabolism and developing novel biotechnological solutions.












