Analytical Data
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Gene name
Viperin
- Application
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Alternative Names
Viperin;CIG5;S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
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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
Q8WXG1
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Expression Region
1-361aa
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AA Sequence
MWVLTPAAFA GKLLSVFRQP LSSLWRSLVP LFCWLRATFW LLATKRRKQQ LVLRGPDETK EEEEDPPLPT TPTSVNYHFT RQCNYKCGFC FHTAKTSFVL PLEEAKRGLL LLKEAGMEKI NFSGGEPFLQ DRGEYLGKLV RFCKVELRLP SVSIVSNGSL IRERWFQNYG EYLDILAISC DSFDEEVNVL IGRGQGKKNH VENLQKLRRW CRDYRVAFKI NSVINRFNVE EDMTEQIKAL NPVRWKVFQC LLIEGENCGE DALREAERFV IGDEEFERFL ERHKEVSCLV PESNQKMKDS YLILDEYMRF LNCRKGRKDP SKSILDVGVE EAIKFSGFDE KMFLKRGGKY IWSKADLKLD W
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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
Viperin, an interferon-stimulated gene (ISG), plays a crucial role in the innate immune response against viral infections. Discovered in the context of antiviral defense, Viperin is known for its ability to inhibit the replication of various viruses, including enveloped viruses such as HIV, West Nile virus, and influenza. Its mechanism of action involves the alteration of lipid metabolism, leading to the production of specific metabolites that interfere with viral life cycles. The recombinant expression of Viperin provides a valuable tool for studying its antiviral properties, molecular mechanisms, and potential therapeutic applications. Researchers aim to better understand Viperin's structure-function relationships and the signaling pathways involved in its induction and activity. This research is critical not only for elucidating Viperin's role in immune responses but also for developing novel antiviral strategies and therapeutics in the face of emerging infectious diseases. As viral threats continue to evolve, the study of Viperin and its recombinantly expressed variants may offer new insights into host defense mechanisms and pave the way for innovative approaches in combating viral pathogens.











