2'-5'-Oligoadenylate Synthetase 2 (OAS2) Antibody

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Description
OAS2 Antibody is a Rabbit Polyclonal against OAS2.
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Product specifications
Category | Primary Antibodies |
Immunogen Target | 2'-5'-Oligoadenylate Synthetase 2 (OAS2) |
Host | Rabbit |
Reactivity | Human, Mouse |
Recommended Dilution | ELISA: 1/1000 - 1/2000, WB: 1/200 - 1/1000. Optimal dilutions/concentrations should be determined by the end user. |
Clonality | Polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Purification | Antigen Affinity Chromatography. |
Size 1 | 50 µl |
Size 2 | 100 µl |
Form | Liquid |
Tested Applications | ELISA, WB |
Buffer | PBS, pH 7.4, containing 0.05% NaN3 and 40% Glycerol. |
Availability | Shipped within 5-10 working days. |
Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
UniProt ID | P29728 |
Gene ID | 4939 |
Background | Antibody anti-OAS2 |
Status | RUO |
Descripción
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OAS2 antibody
Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates(2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L(RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L.
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OAS2 antibody
Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates(2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L(RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L.
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