2',5'-Oligoadenylate Synthetase 1, 40/46kDa (OAS1) Peptide

Details for Product No. ABIN495203
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Protein Name
Synonyms OIAS, IFI-4, OIASI, OAS1, Oas1, Oas1g, Flv, L1, Mmu-L1, Oias-2, Oias2, Wnv
Control Peptide (CP)
Pubmed 5 references available
Catalog no. ABIN495203
Quantity 0.1 mg
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Specificity OAS1 Antibody (C-term) Blocking Peptide
Alternative Name OAS1 / OIAS
Background OAS1 is an interferon inducible protein that may play a role in mediating resistance to virus infection, control of cell growth, differentiation, and apoptosis. It binds double-stranded RNA and polymerizes ATP into PPP(A2'P5'A)N oligomers, which activate the latent RNase L that, when activated, cleaves single-stranded RNAs. This protein is associated with different subcellular fractions such as mitochondrial, nuclear, and rough/smooth microsomal fractions.
Alternate names: (2-5')oligo(A) synthetase 1, 2'-5'-oligoadenylate synthetase 1, 2-5A synthetase 1, p46/p42 OAS
Molecular Weight 1791.42 Da.
Gene ID 4938
NCBI Accession NP_001027581.1
UniProt P00973

This peptide is for ABIN358716

Restrictions For Research Use only
Format Lyophilized
Reconstitution Restore with 0.1 mL deionized water
Concentration 1,0 mg/mL
Buffer Lyophilized with 100% acetonitrile
Handling Advice Avoid repeated freezing and thawing.
Storage 4 °C/-20 °C
Storage Comment Prior to reconstitution store at 2-8°C. Following reconstitution store undiluted at 2-8°C for one month or (in aliquots) at-20°C for longer.
Expiry Date 12 months
Background publications Ghosh, Kusari, Bandyopadhyay et al.: "Cloning, sequencing, and expression of two murine 2'-5'-oligoadenylate synthetases. Structure-function relationships." in: The Journal of biological chemistry, Vol. 266, Issue 23, pp. 15293-9, 1991 (PubMed).

Rutherford, Hannigan, Williams: "Interferon-induced binding of nuclear factors to promoter elements of the 2-5A synthetase gene." in: The EMBO journal, Vol. 7, Issue 3, pp. 751-9, 1988 (PubMed).

Ghosh, Sarkar, Guo et al.: "Enzymatic activity of 2'-5'-oligoadenylate synthetase is impaired by specific mutations that affect oligomerization of the protein." in: The Journal of biological chemistry, Vol. 272, Issue 52, pp. 33220-6, 1998 (PubMed).

Sarkar, Ghosh, Wang et al.: "The nature of the catalytic domain of 2'-5'-oligoadenylate synthetases." in: The Journal of biological chemistry, Vol. 274, Issue 36, pp. 25535-42, 1999 (PubMed).

Strausberg, Feingold, Grouse et al.: "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 99, Issue 26, pp. 16899-903, 2002 (PubMed).

Reactivities (1)
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