SAB1300335
Anti-OAS3 (C-term) antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
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About This Item
NACRES:
NA.41
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ELISA (i), WB
Citations:
1
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.
UniProt accession no.
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.
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
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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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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