Analytical Data
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基因名
PYR1
- Application
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别名
(ABI1-binding protein 6)(Protein PYRABACTIN RESISTANCE 1)(Regulatory components of ABA receptor 11)
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种属
Arabidopsis thaliana
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表达系统
E. coli
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标签
N- MBP & C- His-Avi
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O49686
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表达区间
1-191aa
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分子量
69.3 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
PYR1 (Pyrabactin Resistance 1) is a key receptor protein involved in the abscisic acid (ABA) signaling pathway in plants, playing a crucial role in regulating various physiological processes, including stress responses and seed germination. The study of PYR1 has gained significant attention due to its potential applications in agricultural biotechnology, particularly in enhancing crop resilience to drought and salinity stress. Recent advancements in genomics and proteomics have paved the way for the characterization of PYR1 and its interaction with other proteins, leading to a better understanding of its function at the molecular level. By exploring the structural features of PYR1 through recombinant protein technology, researchers aim to elucidate its binding mechanisms with ABA and downstream signaling components. This knowledge can contribute to the development of crops with improved stress tolerance, thus addressing challenges posed by climate change and food security. The recombinant expression of PYR1 allows for detailed biochemical analyses, providing insights into its role in plant physiology and potential biotechnological applications for improving crop performance under unfavorable conditions.
