Analytical Data
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基因名
pucL
- Application
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别名
pucL；yunL；Uric acid degradation bifunctional Protein PucL
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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
O32141
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表达区间
1-494aa
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氨基酸序列
MFTMDDLNQMDTQTLTDTLGSIFEHSSWIAERSAALRPFSSLSDLHRKMTGIVKAADRETQLDLIKKHPRLGTKKTMSDDSVREQQNAGLGKLEQQEYEEFLMLNEHYYDRFGFPFILAVKGKTKQDIHQALLARLESERETEFQQALIEIYRIARFRLADIITEKGETQMKRTMSYGKGNVFAYRTYLKPLTGVKQIPESSFAGRDNTVVGVDVTCEIGGEAFLPSFTDGDNTLVVATDSMKNFIQRHLASYEGTTTEGFLHYVAHRFLDTYSHMDTITLTGEDIPFEAMPAYEEKELSTSRLVFRRSRNERSRSVLKAERSGNTITITEQYSEIMDLQLVKVSGNSFVGFIRDEYTTLPEDGNRPLFVYLNISWQYENTNDSYASDPARYVAAEQVRDLASTVFHELETPSIQNLIYHIGCRILARFPQLTDVSFQSQNHTWDTVVEEIPGSKGKVYTEPRPPYGFQHFTVTREDAEKEKQKAAEKCRSLKA
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分子量
64.0 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 research on the pucL recombinant protein centers around its role in the Photosynthetic Unit of certain bacteria and its potential applications in biotechnology. PucL, a key component of the light-harvesting complex, is primarily found in purple bacteria, where it assists in capturing light energy for photosynthesis. Understanding the structure and function of pucL is crucial as it can contribute to the development of efficient bioenergy solutions and enhance our comprehension of photosynthetic processes. Recent advancements in molecular biology techniques have enabled the production of recombinant pucL, allowing researchers to analyze its properties in detail. This recombinant protein can be used for various applications, including the design of biosensors, the bioengineering of photosynthetic organisms, and the exploration of synthetic biology approaches to improve energy capture in non-photosynthetic bacteria. Moreover, the study of pucL may shed light on evolutionary processes in photosynthetic systems, providing insights into how these mechanisms have adapted over time. As the global demand for sustainable energy sources rises, the investigation of proteins like pucL stands as a promising avenue for developing innovative technologies that harness solar energy efficiently and sustainably.
