Analytical Data
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Gene name
OASL
- Application
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Alternative Names
OASL；TRIP14；2'-5'-oligoadenylate synthase-like Protein
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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
Q15646
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Expression Region
2-514aa
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AA Sequence
ALMQELYSTPASRLDSFVAQWLQPHREWKEEVLDAVRTVEEFLRQEHFQGKRGLDQDVRVLKVVKVGSFGNGTVLRSTREVELVAFLSCFHSFQEAAKHHKDVLRLIWKTMWQSQDLLDLGLEDLRMEQRVPDALVFTIQTRGTAEPITVTIVPAYRALGPSLPNSQPPPEVYVSLIKACGGPGNFCPSFSELQRNFVKHRPTKLKSLLRLVKHWYQQYVKARSPRANLPPLYALELLTIYAWEMGTEEDENFMLDEGFTTVMDLLLEYEVICIYWTKYYTLHNAIIEDCVRKQLKKERPIILDPADPTLNVAEGYRWDIVAQRASQCLKQDCCYDNRENPISSWNVKRARDIHLTVEQRGYPDFNLIVNPYEPIRKVKEKIRRTRGYSGLQRLSFQVPGSERQLLSSRCSLAKYGIFSHTHIYLLETIPSEIQVFVKNPDGGSYAYAINPNSFILGLKQQIEDQQGLPKKQQQLEFQGQVLQDWLGLGIYGIQDSDTLILSKKKGEALFPAS
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Molecular Weight
66.5 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
The research on OASL (2',5'-oligoadenylate synthetase-like) recombinant proteins has gained significant attention due to their potential role in the immune response and antiviral defense mechanisms. OASL is a member of the OAS family, which is involved in the synthesis of 2',5'-oligoadenylates in response to viral infections. These oligoadenylates play a crucial role in activating RNase L, leading to the degradation of viral RNA and limiting viral replication. Unlike its canonical counterparts, OASL does not possess enzymatic activity; however, it has been shown to modulate immune responses and influence inflammation. Recent studies have indicated that OASL may have implications in various diseases, including cancer and autoimmune disorders, making it a target of interest for therapeutic interventions. The ability to produce recombinant OASL proteins allows researchers to explore their structure-function relationships, interactions with other immune molecules, and their potential as biomarkers for disease diagnosis or prognosis. Understanding the biology of OASL through recombinant proteins can provide insights into its regulatory roles in immune pathways and enhance the development of novel antiviral and immunomodulatory therapies.
