Evidence map›Paper›PMID 25358004›Full record

ArticleMonoclonal antibodies in immunodiagnosis and immunotherapy2014

Development of monoclonal antibodies specifically recognizing the endogenous sterile alpha motif and HD domain 1 protein in porcine cell lines.

Shen Yang, Yan-Jun Zhou, Yuan Zhan, Ling-Xue Yu, Yi-Feng Jiang, Wu Tong, Guang-Zhi Tong

Abstract read
In one paragraph

Article in Monoclonal antibodies in immunodiagnosis and immunotherapy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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0cells of the map it votes in
1citing papers in PubMed
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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

7 authors.

Shen YangShanghai Veterinary Research Institute , Chinese Academy of Agricultural Sciences, Shanghai, P.R. China .
Yan-Jun Zhou
Yuan Zhan
Ling-Xue Yu
Yi-Feng Jiang
Wu Tong
Guang-Zhi Tong

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The sterile alpha motif and HD domain 1 (SAMHD1) protein has been identified as a novel innate immunity restriction factor that participates in processes crucial to the viral life cycle. In the present study, we describe a procedure to generate monoclonal antibodies (MAbs) against porcine SAMHD1 and investigate its characteristics to analyze the expression of endogenous SAMHD1. The open reading frame of porcine SAMHD1 was cloned into the prokaryotic expression vector pCold-TF DNA to construct a recombinant plasmid pcold-pSAMHD1 and induce expression of recombinant porcine SAMHD1 protein by IPTG in Escherichia coli Rosetta. The purified recombinant porcine SAMHD1 protein was used to prepare MAbs of SAMHD1. After subcloning five times hybridoma cell clones expressing SAMHD1, MAbs were generated. Western blot analysis and indirect immunofluorescence assay showed that the overexpressed porcine SAMHD1 in 293T cells and endogenous SAMHD1 protein in porcine cell lines could be specifically recognized by the MAbs produced in this study. In conclusion, specific MAbs of porcine SAMHD1 are reported, and these MAbs provide a valuable tool for further studies of SAMHD1-mediated signaling in virus-infected cells to elucidate the underlying antiviral mechanism.

Indexed as

AnimalsAntibodies, MonoclonalAntibody SpecificityCell LineCell Line, TumorEscherichia coliHEK293 CellsHeLa CellsHumansHybridomasMonomeric GTP-Binding ProteinsOpen Reading FramesRecombinant ProteinsSwineAntibodies, MonoclonalMonomeric GTP-Binding ProteinsRecombinant Proteins

Identifiers

PMID25358004
PMCPMC4216520

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.