Analytical Data
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基因名
p30
- Application
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别名
p30；RNASEP2；Ribonuclease P Protein subunit p30
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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
O14931-1
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表达区间
19-135aa
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氨基酸序列
LWVSQPPEIRTLEGSSAFLPCSFNASQGRLAIGSVTWFRDEVVPGKEVRNGTPEFRGRLAPLASSRFLHDHQAELHIRDVRGHDASIYVCRVEVLGLGVGTGNGTRLVVEKEHPQLG
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分子量
41.8 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
The P30 protein, derived from various plant viruses, has garnered significant attention in the field of molecular biology and plant pathology due to its multifaceted roles in viral replication and host interaction. This protein is particularly notable for its involvement in viral movement within plant tissues, facilitating the spread of the virus and enhancing pathogenicity. Studies have shown that P30 can interact with host proteins, modulating the plant's immune responses and allowing the virus to evade detection. Researchers have focused on understanding the molecular mechanisms underlying these interactions, as well as the potential applications of P30 in biotechnology, such as developing disease-resistant plant varieties or using it as a tool for protein engineering. Furthermore, the expression and characterization of P30 as a recombinant protein have been explored to elucidate its structure-function relationships and to investigate its potential as a target for antiviral strategies. This research has far-reaching implications not only for combating viral infections in crops but also for advancing our knowledge of plant-virus interactions and enhancing agricultural productivity.
