Analytical Data
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Gene name
egfp
- Application
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Alternative Names
egfp；CREME9；CRLM9；CYTOR4；Cytokine receptor-like factor 3
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Species
Human
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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
C5MKY7
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Expression Region
1-239aa
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AA Sequence
MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMDELYK
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Molecular Weight
28.4 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
The enhanced Green Fluorescent Protein (eGFP) has become a pivotal tool in molecular and cellular biology since its introduction as an improved variant of the original Green Fluorescent Protein (GFP) derived from the jellyfish Aequorea victoria. eGFP exhibits increased brightness and stability, making it a preferred marker for visualizing and tracking cellular processes in live cells. Researchers utilize eGFP in a wide range of applications, including gene expression studies, protein localization, and dynamic imaging of cellular interactions. Its non-toxic nature allows for the observation of biological processes in real time without disrupting cellular function. The versatility of eGFP has led to its incorporation into various experimental techniques such as fluorescence microscopy, flow cytometry, and live-cell imaging. Moreover, advancements in eGFP technology have enabled the development of fusion proteins, where eGFP is linked to other proteins of interest, facilitating the study of protein interactions and dynamics within the cellular environment. As research continues to expand, the application of eGFP in genetic engineering, transgenic organisms, and drug discovery remains significant, highlighting its role as a vital tool in advancing our understanding of complex biological systems.
