Analytical Data
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基因名
petE
- Application
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别名
petE；Plastocyanin minor isoform. chloroplastic
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种属
E.coli
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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
P50057
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表达区间
35-131aa
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氨基酸序列
ATVQIKMGTDKYAPLYEPKALSISAGDTVEFVMNKVGPHNVIFDKVPAGESAPALSNTKLAIAPGSFYSVTLGTPGTYSFYCTPHRGAGMVGTITVE
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分子量
26.2 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 petE recombinant protein has gained significant attention due to its role in various biochemical processes involving electron transport and energy conversion in photosynthetic organisms. PetE, a small soluble protein found in the thylakoid membranes of chloroplasts, plays a crucial role in the transfer of electrons from plastocyanin to photosystem I, facilitating efficient photosynthesis. Understanding the structure and function of petE is essential for elucidating the intricate mechanisms of photosynthesis and its regulation. Advances in biotechnology have enabled the production of recombinant petE, allowing researchers to investigate its properties in vitro. These studies aim to explore petE's interactions with other proteins, its stability under varying conditions, and its potential applications in bioengineering and renewable energy. Enhancing our knowledge of petE could provide insights into optimizing photosynthetic efficiency and developing improved crops, thus contributing to global food security and sustainable agricultural practices. Given the urgency of addressing climate change and energy demands, research on petE recombinant protein is not only scientifically significant but also holds promise for practical applications in biotechnological advancements.
