Analytical Data
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基因名
PR-10
- Application
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别名
PR-10；KIAA1231；PFM7；TRIS；PR domain zinc finger Protein 10
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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
P26987
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表达区间
1-158aa
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氨基酸序列
MGVFTFEDEINSPVAPATLYKALVTDADNVIPKALDSFKSVENVEGNGGPGTIKKITFLEDGETKFVLHKIESIDEANLGYSYSVVGGAALPDTAEKITFDSKLVAGPNGGSAGKLTVKYETKGDAEPNQDELKTGKAKADALFKAIEAYLLAHPDYN
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分子量
18.8 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
PR-10 proteins, belonging to the pathogenesis-related (PR) protein group, are primarily associated with plant defense mechanisms against biotic and abiotic stressors. These proteins were first identified in plants like tobacco and wheat, where they exhibit significant expression levels in response to various environmental challenges, such as pathogen attacks or extreme temperatures. Their role in plant defense is attributed to their ability to possess ribonuclease and antimicrobial activities, enhancing the resistance of plants to pathogens. The study of PR-10 proteins has gained momentum due to their potential applications in agriculture and biotechnology, particularly in developing disease-resistant crop varieties and understanding plant immunity at a molecular level. Moreover, the structural properties of PR-10 proteins, which often exhibit a stable fold conducive to various functions, have made them a subject of interest for recombinant protein engineering. This research aims to explore the functional versatility of PR-10 proteins, including their potential for use in pharmaceuticals and biocontrol agents, tapping into their inherent properties to create innovative solutions for challenges in crop production and plant health management. As agricultural practices evolve in the face of climate change and increasing pest resistance, understanding and harnessing PR-10 proteins could provide critical insights and tools for sustainable agriculture.
