Analytical Data
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Gene name
D1
- Application
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Alternative Names
NaD1
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Species
Nicotiana alata
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8GTM0
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Expression Region
26-72aa
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Molecular Weight
21.3 kDa
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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
D1 recombinant proteins, often derived from plant or microbial systems, play a crucial role in various fields, including biotechnology, pharmaceuticals, and agriculture. The D1 protein is a pivotal component of photosystem II in higher plants, where it participates in the light-dependent reactions of photosynthesis. Its significance extends beyond basic scientific inquiry; D1 has implications for enhancing agricultural productivity, developing biofuels, and understanding plant stress responses. Research into D1 recombinant proteins aims to elucidate their structure-function relationships, enabling scientists to manipulate these proteins for improved efficiency in photosynthesis or to create crops that can withstand environmental stressors such as drought or salinity. Moreover, advancements in genetic engineering techniques have facilitated the production of D1 proteins with tailored characteristics, paving the way for innovations in crop improvement and sustainable agriculture. Investigating D1 recombinant proteins not only enhances our understanding of plant biology but also contributes to the development of biotechnological solutions that address global challenges, such as food security and climate change. Thus, the study of D1 recombinant proteins is a significant area of research that intertwines structural biology, genetics, and environmental science, ultimately aiming for a more sustainable future.
