Analytical Data
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基因名
PDF1.2A
- Application
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别名
Low-molecular-weight cysteine-rich protein 77
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种属
Arabidopsis thaliana
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表达系统
E. coli
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标签
Tag Free
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9FI23
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表达区间
30-80aa
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分子量
5.5 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
PDF1.2A is a protein that has garnered significant attention in the field of plant biology and biotechnology due to its role in stress response mechanisms. Derived from the plant Arabidopsis thaliana, this recombinant protein is particularly interesting because it is associated with plant defense against biotic and abiotic stresses, including pathogen attack and environmental challenges such as drought and salinity. Research into PDF1.2A has revealed its involvement in the synthesis of antimicrobial compounds, which contribute to the plant’s resilience and survival. The study of this protein also offers insights into the molecular pathways that underpin plant immunity, making it a valuable target for genetic engineering aimed at enhancing crop resistance to various stresses. Furthermore, the recombinant expression of PDF1.2A in model systems allows scientists to explore its biochemical properties and functional mechanisms, paving the way for potential applications in agricultural biotechnology. As global challenges such as climate change and food security intensify, understanding and harnessing the biological functions of proteins like PDF1.2A could lead to the development of stress-resistant crops, thereby contributing to sustainable agricultural practices and food production.
