Analytical Data
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Gene name
petE
- Application
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Alternative Names
petE；Plastocyanin minor isoform. chloroplastic
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P50057
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Expression Region
35-131aa
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AA Sequence
ATVQIKMGTDKYAPLYEPKALSISAGDTVEFVMNKVGPHNVIFDKVPAGESAPALSNTKLAIAPGSFYSVTLGTPGTYSFYCTPHRGAGMVGTITVE
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Molecular Weight
26.2 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
The study of petE recombinant protein has gained significant attention due to its role in various biochemical processes involving electron transport and energy conversion in photosynthetic organisms. PetE, a small soluble protein found in the thylakoid membranes of chloroplasts, plays a crucial role in the transfer of electrons from plastocyanin to photosystem I, facilitating efficient photosynthesis. Understanding the structure and function of petE is essential for elucidating the intricate mechanisms of photosynthesis and its regulation. Advances in biotechnology have enabled the production of recombinant petE, allowing researchers to investigate its properties in vitro. These studies aim to explore petE's interactions with other proteins, its stability under varying conditions, and its potential applications in bioengineering and renewable energy. Enhancing our knowledge of petE could provide insights into optimizing photosynthetic efficiency and developing improved crops, thus contributing to global food security and sustainable agricultural practices. Given the urgency of addressing climate change and energy demands, research on petE recombinant protein is not only scientifically significant but also holds promise for practical applications in biotechnological advancements.
