Analytical Data
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Gene name
psaA
- Application
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Alternative Names
psaA；Photosystem I P700 chlorophyll a apoProtein A1
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Species
Streptococcus
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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
P0A4G3
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Expression Region
20-309aa
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AA Sequence
CASGKKDTTSGQKLKVVATNSIIADITKNIAGDKIDLHSIVPIGQDPHEYEPLPEDVKKTSEADLIFYNGINLETGGNAWFTKLVENAKKTENKDYFAVSDGVDVIYLEGQNEKGKEDPHAWLNLENGIIFAKNIAKQLSAKDPNNKEFYEKNLKEYTDKLDKLDKESKDKFNKIPAEKKLIVTSEGAFKYFSKAYGVPSAYIWEINTEEEGTPEQIKTLVEKLRQTKVPSLFVESSVDDRPMKTVSQDTNIPIYAQIFTDSIAEQGKEGDSYYSMMKYNLDKIAEGLAK
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Molecular Weight
40.0 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 recombinant psaA protein has gained significant attention due to its crucial role in the photosynthetic machinery of various cyanobacteria and autotrophic organisms. PsaA is a core component of the Photosystem I (PSI) complex, involved in light harvesting and electron transport, playing a pivotal part in the energy conversion processes essential for photosynthesis. Understanding the structure and function of psaA is vital, as it can provide insights into the efficiency of photosynthesis and the broader implications for bioenergy and agriculture. Researchers are increasingly focusing on the recombinant expression of psaA to obtain higher yields of pure protein for biophysical and biochemical analyses. These studies help elucidate the protein's interaction with other components of the PSI complex and its response to environmental stressors, thereby contributing to the development of genetically engineered plants and microorganisms with improved photosynthetic efficiency. Moreover, as global energy demands rise and concerns about climate change grow, harnessing the potential of psaA through recombinant technologies could lead to novel strategies for sustainable energy production.
