Analytical Data
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Gene name
CFP
- Application
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Alternative Names
CFP；PFC；Properdin
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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
P27918
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Expression Region
213-334aa
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AA Sequence
PHEPKETRSRKCSAPEPSQKPPGKPCPGLAYEQRRCTGLPPCPVAGGWGP WGPVSPCPVTCGLGQTMEQRTCNHPVPQHGGPFCAGDATRTHICNTAVPC PVDGEWDSWGEWSPCIRRNMKS
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Molecular Weight
39 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 CFP (Cyan Fluorescent Protein) recombinant proteins has garnered increasing attention due to their significant applications in molecular and cellular biology. Originally derived from the marine organism, the Aequorea victoria jellyfish, CFP exhibits unique fluorescence properties that make it an invaluable tool for visualizing cellular processes in live organisms. Researchers employ CFP as a reporter protein in various applications, including gene expression studies, protein-protein interaction assays, and cellular localization investigations. The ability to tag proteins with CFP allows scientists to monitor dynamic biological processes in real-time, facilitating the understanding of complex signaling pathways and genetic functions. Furthermore, advancements in genetic engineering techniques have enabled the optimization of CFP variants, enhancing their brightness and stability, thus broadening their utility. As a result, the exploration of CFP recombinant proteins is a vital area of research, contributing to our knowledge in fields such as developmental biology, neuroscience, and cancer research. This ongoing research not only aids in deciphering fundamental biological mechanisms but also has implications for biomedical applications, including drug discovery and the development of therapeutic strategies.
