Analytical Data
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Gene name
Luciferase
- Application
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Species
PHOPY
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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
P08659
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Expression Region
1-550aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMMEDAKNIKKGPAPFYPLEDGTAGEQLHKA MKRYALVPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIV VCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVS KKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPPGFNEY DFVPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGN QIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQD YKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAK RFHLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDTG KTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDED EHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGE LPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGK LDARKIREILIKAKKGGKIAV
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Molecular Weight
63 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
Luciferase is an enzyme that catalyzes bioluminescence, a natural phenomenon primarily observed in certain species of fireflies and other bioluminescent organisms. The study of recombinant luciferase protein has gained significant attention due to its applications in various fields, including molecular biology, biochemistry, and biotechnology. Researchers have employed luciferase as a powerful reporter gene in gene expression studies, allowing for real-time monitoring of cellular processes and gene activation due to its high sensitivity and rapid kinetics. Different types of luciferases, such as Firefly luciferase (FLuc) and Renilla luciferase (RLuc), are often used in dual-luciferase assays to provide a means for normalization and comparative analysis of gene expression. Furthermore, advancements in genetic engineering have enabled the development of modified luciferases with enhanced properties, such as improved stability, altered emission spectra, and increased luminescence intensity. This versatility not only facilitates diverse experimental designs but also expands the potential for diagnostic applications and in vivo imaging in live organisms. Overall, research into recombinant luciferase proteins continues to evolve, driving innovation in both fundamental research and clinical applications.
