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SAB1300335

Sigma-Aldrich

Anti-OAS3 (C-term) antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human

technique(s)

indirect ELISA: 1:1000
western blot: 1:100-1:500

NCBI accession no.

NP_006178

UniProt accession no.

Q9Y6K5

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... OAS3(4940)

General description

OAS3 is an interferon inducible protein that belongs to the 2-5A synthetase family, may play a role in mediating resistance to virus infection, control of cell growth, differentiation, and apoptosis. OAS3 synthesizes preferentially dimeric 2′,5′-oligoadenylate molecules. GTP can be an alternative substrate. OAS3 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. The protein is present at high level in placenta trophoblast.

Immunogen

OAS3 (Q9Y6K5, 1060-1097)
This antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the C-terminal region of human OAS3.

Physical form

Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide.

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Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Huijing Yin et al.
Cell death & disease, 10(9), 642-642 (2019-09-11)
RNase L is an essential component in interferon (IFN)-mediated antiviral signaling that showed antitumor effects in cancer. Cancer immunotherapy based on interferon has achieved encouraging results that indicate an applicable potential for cancer therapy. Here we showed that function of

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