Related Experiment Video
Updated: May 11, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
Characterization of the optimized C2 domain of protein G: finding its additional chicken IgY-binding ability
Yongsheng Cao1, Di Li, Chong Cao
1College of Veterinary Medicine, Northeast Agricultural University, Harbin, 150030, People's Republic of China. caoys87@sina.com.cn
Abstract:
The C2 domain of streptococcal protein G is a small (55 residue) peptide with immunoglobulin-binding activity. Following codon optimization, the gene was divided into four oligonucleotide fragments and amplified by overlap PCR. The recombinant plasmid pET30a-C2 was transformed into Escherichia coli Rosetta (DE3) PLysS for expression. After purification by Ni-NTA, the fusion protein was identified by western-blotting, Dot-ELISA and ELISA. His-tagged C2 bound to human, rabbit, cattle, pig, goat, mouse or guinea pig IgG had no affinity for goose, duck, wild duck, wild turkey and red-crowned crane IgY. Its affinity for chicken IgY, however, was comparable to that of guinea pig IgG. The C2 domain may therefore provide an ideal material for the purification and detection of immunoglobulin G from various mammals.
More Related Videos
11:42High Yield Expression of Recombinant Human Proteins with the Transient Transfection of HEK293 Cells in Suspension
Published on: December 28, 2015
10:33Isolation and Characterization Of Chimeric Human Fc-expressing Proteins Using Protein A Membrane Adsorbers And A Streamlined Workflow
Published on: January 8, 2014
Related Concept Videos
Antibody Structure
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibody Structure
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Immunoglobulin-like Cell Adhesion Molecules
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Antibody Structure and Classes
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.