Analytical Data
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基因名
pucL
- Application
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别名
2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase;OHCU decarboxylase;Uricase;Urate oxidase
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种属
Bacillus subtilis
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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
O32141
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表达区间
1-494aa
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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
PucL recombinant protein has garnered significant attention in molecular biology and biotechnology due to its pivotal role in various biological processes. Originally identified as a component of the photochemical apparatus of purple bacteria, PucL is part of the light-harvesting complexes that facilitate photosynthesis by effectively capturing light energy and transferring it to reaction centers. The study of PucL and its recombinant forms has crucial implications for understanding the mechanisms of energy transfer and conversion in photosynthetic organisms. Researchers have aimed to express PucL in heterologous systems, allowing for detailed structural and functional analyses, which can unveil the nuances of its interactions with other proteins. Additionally, the characterization of the PucL protein may aid in the development of bioengineering applications, including the design of more efficient solar energy harvesting systems and advancements in synthetic biology. Given the increasing global demand for sustainable energy solutions, the exploration of PucL and its properties can contribute to innovative approaches in bioenergy production and environmental sustainability. Thus, the ongoing research into PucL recombinants not only enhances our fundamental understanding of photosynthesis but also opens avenues for applied research with potential economic and ecological benefits.
