Analytical Data
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Gene name
PRF
- Application
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Alternative Names
PRF；HDBP2；PBF；Zinc finger Protein 395
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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
Q58NA1
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Expression Region
2-163aa
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AA Sequence
SDWDPVVKEWLVDTGYCCAGGIANAEDGVVFAAAADDDDGWSKLYKDDHEEDTIGEDGNACGKVSINEASTIKAAVDDGSAPNGVWIGGQKYKVVRPEKGFEYNDCTFDITMCARSKGGAHLIKTPNGSIVIALYDEEKEQDKGNSRTSALAFAEYLHQSGY
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Molecular Weight
19.4 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
Related Products
Protein Description
PRF (Protein Recombination Factor) recombinant proteins have gained considerable attention in the field of molecular biology and biotechnology due to their pivotal role in various cellular processes, including DNA repair, gene expression regulation, and signal transduction. The ability to manipulate and produce these proteins through recombinant DNA technology has unveiled new dimensions in understanding their functional mechanisms and interactions within cellular contexts. Studies have demonstrated that PRF proteins are not only crucial for maintaining genomic stability but also play significant roles in the pathogenesis of several diseases, including cancer and autoimmune disorders. By utilizing techniques such as CRISPR/Cas9 for gene editing and advanced expression systems for protein production, researchers aim to elucidate the structure-function relationships of PRF proteins. This research trajectory not only aims to unravel the complexities of PRF interactions but also explores their potential as innovative therapeutic targets. With advancements in proteomics and structural biology, the comprehensive study of PRF recombinant proteins promises to enhance our understanding of cellular dynamics and the development of novel strategies for disease intervention. The ongoing investigations are poised to contribute significantly to both academic knowledge and practical applications in medicine and biotechnology.
