Analytical Data
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Gene name
LCY1
- Application
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Alternative Names
LCY1；CRTL；Lycopene beta cyclase. chloroplastic/chromoplastic
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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
Q38933
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Expression Region
81-501aa
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AA Sequence
QVVDLAIVGGGPAGLAVAQQVSEAGLSVCSIDPSPKLIWPNNYGVWVDEFEAMDLLDCLDTTWSGAVVYVDEGVKKDLSRPYGRVNRKQLKSKMLQKCITNGVKFHQSKVTNVVHEEANSTVVCSDGVKIQASVVLDATGFSRCLVQYDKPYNPGYQVAYGIVAEVDGHPFDVDKMVFMDWRDKHLDSYPELKERNSKIPTFLYAMPFSSNRIFLEETSLVARPGLRMEDIQERMAARLKHLGINVKRIEEDERCVIPMGGPLPVLPQRVVGIGGTAGMVHPSTGYMVARTLAAAPIVANAIVRYLGSPSSNSLRGDQLSAEVWRDLWPIERRRQREFFCFGMDILLKLDLDATRRFFDAFFDLQPHYWHGFLSSRLFLPELLVFGLSLFSHASNTSRLEIMTKGTVPLAKMINNLVQDRD
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Molecular Weight
49.1 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
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Protein Description
LCY1, or Lycoris Complex I-like protein 1, has emerged as a significant focus of research due to its potential role in various biological processes, including cellular energy metabolism and signal transduction. Found predominantly in certain plant species, LCY1 has been linked to the functioning of the mitochondrial respiratory chain, particularly in its involvement in the complex I assembly and stability. Understanding its structure and function can provide insights into the mechanisms underlying plant development and stress responses. Recent studies have indicated that LCY1 may have implications in agricultural biotechnology, especially in enhancing crop resilience to environmental stressors. Additionally, its evolutionary significance in relation to other complex I components invites further exploration of its functionalities across different organisms. As the demand for sustainable agricultural practices grows, elucidating the role of LCY1 could contribute to developing innovative strategies aimed at improving plant performance under adverse conditions. Therefore, ongoing research on LCY1 recombinant proteins aims to characterize their biochemical properties, interactions, and regulatory mechanisms, leading to practical applications in crop improvement and sustainability efforts.
