Analytical Data
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Gene name
NPHP5
- Application
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Alternative Names
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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Species
Mouse
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8BP00
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Expression Region
Leu317~Pro598
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Molecular Weight
64kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
Related Products
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.
