Analytical Data
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Gene name
GFP
- Application
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Alternative Names
GFPGreen fluorescent protein
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Species
Jellyfish
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P42212
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Expression Region
1-238aa
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Molecular Weight
28.9 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
Green Fluorescent Protein (GFP) was first discovered in the jellyfish Aequorea victoria and has since become a fundamental tool in molecular and cell biology. Its unique fluorescent properties, resulting from its chromophore formed through post-translational modifications, allow researchers to visualize and track proteins within living cells and organisms without the need for external substrates. The development of GFP and its variants, which exhibit a spectrum of fluorescence colors, has revolutionized the fields of microscopy, gene expression analysis, and protein localization studies. GFP-tagged recombinant proteins facilitate the real-time observation of dynamic biological processes, enabling scientists to probe cellular functions, protein interactions, and trafficking pathways. Additionally, the ability to express GFP in various model organisms has expanded the applications of GFP-based studies to developmental biology, neuroscience, and plant biology. Researchers continue to explore innovative applications of GFP and its derivatives, addressing challenges such as photobleaching and achieving deeper tissue imaging in living systems. As a versatile and powerful tool, GFP remains crucial in advancing our understanding of cellular dynamics and protein functionality in various biological contexts.
