Immunoglobulins, also known as antibodies, are the firstly characterized molecules involved in specific immune recognition. In recent decades, the success of antibody therapy in the fields of hematology, oncology, autoimmune diseases, and infections is consistent with the ability of these molecules to activate immune responses. Compared with classical IgG, IgE presents great potential as a therapeutic agent. Based on years of experience, now Creative Biolabs can provide our worldwide clients with professional IgE production and purification services based on the value of quality.
Introduction of IgE
IgE is a type of antibody isotype that only has been found in mammals. Synthesized by plasma cells, IgE antibodies have a different structure compared with the conventional IgG1 antibodies. As shown in Fig.1, the heavy chain of IgG contains 3 constant domains, while the IgE heavy chain has a total of 4 constant domains. As for the light chain, both of them have 1 variable and 1 constant domain. IgEs are the least abundant circulating antibodies in the serum because of the short half-life (1-3 days compared to 3 weeks of IgG) and the small number of IgE-secreting plasma cells.
IgE antibody mediates different biological functions by binding to two Fc receptors: the high-affinity receptor, FcεRI, and the low-affinity receptor, FcεRII. The expression of these two Fcε receptors can be upregulated by IgE antibody under certain cases. Compared to IgG, IgE antibodies present several properties that make them attractive as excellent cancer therapeutics.
One of the most important points is the high affinity to its FcεRs, the main effector receptors for immune response, allergic reactions, and anti-tumor effects of IgE antibody. In addition, the unique effector cells involved in the allergic reaction show promising advantages of IgE-based cancer therapies. Low endogenous blood levels of IgE antibody enable less competition for receptor occupancy. In contrast to IgG1, IgE does not activate the complement pathway and thereby is unable to induce the complement-dependent cytotoxicity effect.
Fig.1 Schematic diagram comparing the structures of human IgE and IgG1. (Leoh, 2015)
To obtain high-quality antibodies for further researches and clinical applications, Creative Biolabs produces IgE antibodies by signal cell cloning based on our advanced Expression System Platform. Once the sequence or antigen is provided, we can start with gene synthesis, vector construction, and plasmid preparation. After the subsequent transient transfection, selection and, cloning, the IgE antibodies can be obtained in high yields.
Fig.2 Development of a stable platform for the expression of recombinant IgE. (Crescioli, 2018)
In order to obtain purified IgE, the purification method is really important. The optional purification methods contain affinity chromatography column purification, ion-exchange chromatography, liquid chromatography, size-exclusion chromatography, and a combination of these methods when needed.
Fig.3 A process of our IgE production and purification.
For further investigation and clinical tests of IgE antibody, obtaining high-quality antibodies on a large scale is a prerequisite. Creative Biolabs is an excellent biotech company that provides professional production and purification services of IgE antibody as well as related services based on our extensive experience and advanced platforms.
If you are working on antibodies researches (IgG or non-IgG antibodies), please feel free to contact us for more details.
- Leoh, L.S.; et al. IgE immunotherapy against cancer. Current Topics in Microbiology and Immunology. 2015, 388: 109-149.
- Crescioli, S.; et al. Engineering and stable production of recombinant IgE for cancer immunotherapy and AllergoOncology. The Journal of Allergy and Clinical Immunology. 2018, 141(4): 1519-1523.
!! For Research Use Only. Our products and services are NOT intended for diagnostic or therapeutic applications.