Analytical Data
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Gene name
efp
- Application
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Alternative Names
efp；EFP；RNF147；ZNF147；E3 ubiquitin/ISG15 ligase TRIM25
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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
P0A6N4
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Expression Region
2-188aa
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AA Sequence
ATYYSNDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVVDMNLTYLYNDGEFWHFMNNETFEQLSADAKAIGDNAKWLLDQAECIVTLWNGQPISVTPPNFVELEIVDTDPGLKGDTAGTGGKPATLSTGAVVKVPLFVQIGEVIKVDTRSGEYVSRVK
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Molecular Weight
22.5 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
EFP (Enhancer of Filamentation and Plasmid Maintenance) is a protein that plays a crucial role in various cellular processes, including gene regulation and stress response. Research on EFP and its recombinant form has gained significant attention due to its potential therapeutic applications and implications in understanding cellular mechanisms. EFP is known to interact with specific proteins and DNA elements that regulate transcription, thereby influencing cell growth and differentiation. Moreover, its association with filamentous growth in certain organisms suggests its involvement in stress responses and adaptation. Recombinant EFP proteins are being studied for their ability to modulate signaling pathways and their potential use in biotechnology and medicine. By engineering EFP, researchers aim to explore its functional properties and develop novel strategies for controlling cellular activities, which could lead to advancements in treating diseases such as cancer or metabolic disorders. Understanding the structure-function relationship of EFP and optimizing its recombinant expression can provide insights into its biological significance and pave the way for innovative therapeutic approaches. The continued exploration of EFP in the context of reconstituted proteins underscores its importance in molecular biology and opens avenues for future research in protein engineering and synthetic biology.
