ArticleMonoclonal antibodies in immunodiagnosis and immunotherapy2013
A polyclonal antibody against recombinant bovine haptoglobin expressed in Escherichia coli.
Article in Monoclonal antibodies in immunodiagnosis and immunotherapy, 2013. 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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1 citing paper in PubMed, 1 citations in OpenAlex.
- Preparation of monoclonal antibodies against bovine haptoglobin.Monoclonal antibodies in immunodiagnosis and immunotherapy · 2014Article
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4 authors at 1 institution in 1 country.
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Abstract
The nucleotide sequence of the predicted immunodominant region of bovine haptoglobin (pirBoHp), without the signal peptide sequence, was synthesized based on the codon usage bias of Escherichia coli. The synthesized pirBoHp gene was cloned into the prokaryotic expression vector pET-32a (+), which contains a His-tag. The recombinant pirBoHp protein was successfully expressed in E. coli BL21 (DE3) cells. Western blot analysis showed that the purified recombinant pirBoHp protein could be recognized by an anti-His-tag monoclonal antibody. Further investigations indicated that a polyclonal antibody against the recombinant pirBoHp protein could recognize the α and β chains of native bovine haptoglobin in a pooled plasma sample from dairy cattle suffering from foot rot.
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