Analytical Data
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基因名
NPHP5
- Application
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别名
IQCB1; PIQ; SLSN5; IQ Calmodulin Binding Motif Containing Protein 1; IQ Motif Containing B1; p53 and DNA damage-regulated IQ motif protein
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种属
Mouse
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表达系统
E. coli
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标签
N- His & GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q8BP00
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表达区间
Leu317~Pro598
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分子量
64kDa
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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
NPH5, or Non-Phototropic Hypocotyl 5, is a key protein involved in various physiological processes in plants, particularly in light signaling and photomorphogenesis. Research on the recombinant NPH5 protein has gained attention due to its role in mediating the plant's response to light, affecting growth and development. NPH5 interacts with phytochromes, the light receptors in plants, and has been implicated in regulating gene expression in response to environmental stimuli, thereby influencing seedling orientation and growth patterns. Understanding the structure and function of NPH5 through recombinant protein studies can provide insights into the mechanisms plants use to adapt to their surroundings, including their ability to optimize light capture for photosynthesis. Furthermore, investigations into the biochemical properties and interactions of the NPH5 protein may reveal potential applications in agricultural biotechnology, such as developing crops with improved light utilization efficiency and stress resilience. This research is vital not only for fundamental plant biology but also for addressing challenges in food security and sustainable agriculture in the face of climate change.
