Antibody Development
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Antibody Development
Antibodies are glycoproteins belonging to the immunoglobulin superfamily. Generally, antibodies can be divided into 4 major types based upon their origin and clonality:
1. IgG polyclonal and monoclonal antibodies
Their origin is mammalian B-cells and they are present in blood circulation and lymph nodes.
2. IgY polyclonal and monoclonal antibodies
These are the antibodies also produced by B-cells, but they are secreted into egg yolk.
GenWay's core technology can generate libraries of gene-specific and domain-targeted antibodies, which can be either polyclonal or monoclonal, based upon gene-expression or formulated protein/peptide immunization. GenWay specializes in polyclonal chicken antibodies, which are isolated from the egg yolk of the immunized chickens, and are called IgY (Immunoglobulin Yolk). GenWay also has the know-how and technology to produce mammalian IgG antibodies from rabbit and mouse host systems, in both polyclone and monoclone formats. The antibodies can be directly used for research and diagnostic applications. In meeting the needs of therapeutics or in human application, GenWay has also developed technology and know-how for producing humanized or fully human antibodies.
IgG and IgY are common in many aspects as immunoglobulin. However, they also have definitive differences with associated advantages and
disadvantages (Table 1).
Table 1. Comparison of Antigens |
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| Features of Comparison |
IgG |
IgY |
References |
| Overview | Relatively matured in technology development and application |
Relatively new in product development and application |
Larsson et al., 1993 Warr et al., 1995 Schade and Hlinak 1996 Zhang, 2003 |
| Animal | Mammal | Birds, Reptiles, Amphibia | Klemperer, 1893 Warr et al., 1995 |
| Sources | Serum | Egg Yolk | Patterson et al., 1962 Leslie and Clem, 1969 Du Pasquier et al., 1989 |
| Molecular Weight (by SDS-PAGE) |
Whole: 150 kDa Light chains: 22 kDa x 2 Heavy chains: 50 kDa x 2 |
Whole: 180 kDa Light chains: 21 kDa x 2 Heavy chains: 70 kDa x 2 |
Hatta et al., 1993 |
| Molecular Weight (by MALDI-TOF MS) |
Whole: 150 kDa Light chains: 23 kDa x 2 Heavy chains: 50 kDa x 2 |
Whole: 167 kDa Light chains: 19 kDa x 2 Heavy chains: 65 kDa x 2 |
Sun et al., 2001 |
| Basic Structure Differences |
Flexible hinge region, shorter Fc stem with 1 pairs of carbohydrate groups |
Shorter and less flexible hinge, longer Fc region with 2 pairs of carbohydrate groups |
Warr et al., 1995 |
| Immune Response to Mammalian Antigens |
Adversely affected by phylogenetic homology | Enhanced by phylogenetic differences | Gassmann et al., 1990 |
| Affinity Maturation Mechanism |
Somatic hypermutation | Pseudo-V gene conversion | Bezzubova and Buerstedde 1994 Warr et al., 1995 |
| Affinity or Avidity | Moderate | High | Ikemori et al., 1993 Lemamy et al., 1999 Lin et al., 2001 |
| Quantity (Yield per month per animal) |
Milligrams with 0.1-5% specific antibodies (rabbit) |
Grams with 0.1-10% specific antibodies | Schade et al., 1994 |
| Cross Reactivity | High to human (antibody) | Low to human (antibody) | Hadge et al., 1984 Tini et al., 2002 |
| Non-Affinity Isolation |
Relatively more complicated and slow | Fast and simple | Polson et al., 1980 Akita and Nakai, 1993 Schwarzkopf and Thiele, 1996 Bizhanov and Vyshniauskis, 2000 Stalberg and Larsson, 2001 Devi et al., 2002 |
| Affinity Purification |
Proteins A or G, or antigen-based purification |
Protein L or antigen-based purification | Lin et al., 2001 |
| Stability | Good, Stable at pH 3-10, up to 700C | Good, Stable at pH 4-9, up to 650C | Shimizu et al., 1992 Hatta et al., 1993 Lee et al., 2002 |
| Hydrophobicity | Less hydrophobic than IgY | Fc region is hydrophobic | Davalos-Pantoja et al., 2000 |
| Immunoaffinity Fractionation |
IgG microbeads are shown having less binding capacity and higher non-specific binding |
IgY microbeads are highly specific with high capacity in capturing and removal of highly-abundant proteins. Less non-specific binding |
Fang et al., 2004 Hinerfeld et al., 2004 Huang et al., 2005 Qian et al., 2006 Liu et al., 2006 |
| Productivity | Limited in quantity and duration | High with greater quantity and long duration | Gassmann et al., 1990 Hatta et al., 1993 |
| Scalability | Difficult | Feasible and practical | Mine and Kovacs-Nolan, 2002 |
| Monoclonal Antibodies |
Have been well developed | Several cases reported, technology development is rapidly progressing |
Sasai et al.,1996 Michael et al., 1998 Greunke et al., 2006 Miyamoto et al., 2007 |
| Immune Suppression |
Several products are under development | May be useful for xenotransplantation | Fryer et al., 1999 |
| Diagnosis | Widely used, especially monoclonal antibodies | Useful and practical for various applications | Erhard et al., 2000 Carlander et al., 1999 |
| Therapeutics | Well developed | To be further developed, such as in antibiotic-alternative therapy |
Carlander et al., 2000 Mine and Kovacs-Nolan, 2002 Tsurushita et al., 2004 |
For further information on the features and applications of IgY and IgG antibodies, as well as the related products such as secondary antibodies and antibody conjugates, please visit the pages:
- IgY Polyclonal Antibodies
- IgY Monoclonal Antibodies
- IgG Polyclonal Antibodies
- IgG Monoclonal Antibodies
- Secondary Antibodies
GenWay offers extensive custom services in antibody development and applications. For more detailed information, please see the specific description pages in Custom Antibodies,and Immunoaffinity Separation.