A polyclonal antibody against recombinant bovine haptoglobin expressed in Escherichia coli.

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.

• Authors: Donghua Guo, Hong Zhang, Chunqiu Li, Dongbo Sun
• Journal: Monoclonal antibodies in immunodiagnosis and immunotherapy (Monoclon Antib Immunodiagn Immunother) Vol. 32 Issue 6 Pg. 419-24 (Dec 2013) ISSN: 2167-9436 [Electronic] United States
• PMID: 24328747 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Antibodies
• Haptoglobins
• Recombinant Fusion Proteins

Topics

• Animals
• Antibodies (chemistry)
• Base Sequence
• Blotting, Western
• Cattle
• Escherichia coli
• Haptoglobins (biosynthesis, genetics, immunology)
• Mice
• Mice, Inbred BALB C
• Molecular Sequence Data
• Recombinant Fusion Proteins (biosynthesis, genetics, immunology)