Analytical Data
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Gene name
OAS2
- Application
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Alternative Names
OAS2；2'-5'-oligoadenylate synthase 2
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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
P29728-2
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Expression Region
1-687aa
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AA Sequence
MGNGESQLSSVPAQKLGWFIQEYLKPYEECQTLIDEMVNTICDVLQEPEQ FPLVQGVAIGGSYGRKTVLRGNSDGTLVLFFSDLKQFQDQKRSQRDILDK TGDKLKFCLFTKWLKNNFEIQKSLDGFTIQVFTKNQRISFEVLAAFNALS LNDNPSPWIYRELKRSLDKTNASPGEFAVCFTELQQKFFDNRPGKLKDLI LLIKHWHQQCQKKIKDLPSLSPYALELLTVYAWEQGCRKDNFDIAEGVRT VLELIKCQEKLCIYWMVNYNFEDETIRNILLHQLQSARPVILDPVDPTNN VSGDKICWQWLKKEAQTWLTSPNLDNELPAPSWNVLPAPLFTTPGHLLDK FIKEFLQPNKCFLEQIDSAVNIIRTFLKENCFRQSTAKIQIVRGGSTAKG TALKTGSDADLVVFHNSLKSYTSQKNERHKIVKEIHEQLKAFWREKEEEL EVSFEPPKWKAPRVLSFSLKSKVLNESVSFDVLPAFNALGQLSSGSTPSP EVYAGLIDLYKSSDLPGGEFSTCFTVLQRNFIRSRPTKLKDLIRLVKHWY KECERKLKPKGSLPPKYALELLTIYAWEQGSGVPDFDTAEGFRTVLELVT QYQQLCIFWKVNYNFEDETVRKFLLSQLQKTRPVILDPAEPTGDVGGGDR WCWHLLAKEAKEWLSSPCFKDGTGNPIPPWKVPVKVI
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Molecular Weight
105 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 OAS2 recombinant protein is rooted in its critical role in the innate immune response against viral infections. Oligoadenylate synthase 2 (OAS2) is an enzyme that is part of the OAS family, activated by double-stranded RNA, a common byproduct of viral replication. Upon activation, OAS2 synthesizes 2',5'-linked oligoadenylates, leading to the activation of RNase L, which subsequently degrades viral RNA, thus inhibiting viral replication. There is growing interest in OAS2 due to its potential therapeutic applications in treating viral infections and its involvement in various pathologies, including autoimmune diseases and cancer. By engineering recombinant OAS2 proteins, researchers aim to better understand its structure-function relationships, optimize its antiviral properties, and explore its efficacy in different therapeutic contexts. Recent advancements in molecular biology techniques allow for the production and purification of active OAS2, facilitating detailed biochemical and functional studies. Investigating OAS2 not only enriches our fundamental understanding of viral pathogenesis and host defense mechanisms but also paves the way for novel antiviral strategies and diagnostics. As researchers continue to explore the intricate dynamics of OAS2 and its interactions within the immune system, it holds promise for enhancing our ability to combat a range of viral diseases effectively.
