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Veterinary IgE Fc Proteins

Immunoglobulin (Ig)E is an isotype which has strong protective capacities against some pathogens like parasites and helminths, and deleterious effects in triggering allergic responses due to cytokine release from cells expressing high-affinity IgE receptors. It plays a critical role in allergic reactions and certain autoimmune diseases.

Veterinary IgE Fc Proteins

Immunoglobulin E (IgE) is a type of antibody that has only been found in mammals and is synthesised by plasma cells. IgE is a monomer with four constant regions. Monomers of IgE consist of two heavy chains (ε chain) and two light chains, with the ε chain containing 4 Ig-like constant domains (Cε1-Cε4). IgE is one of the 5 classes of immunoglobulins, and is defined by the presence of the epsilon heavy chain. It is the most recently described immunoglobulin, having first been identified in 1966. IgE exists as a monomer, and is present in circulation at very low concentrations, approximately 300-fold lower than that of IgG. As in all Igs, it has a four-chain structure as its basic unit. It is composed of two identical heavy (50–70 kD) and two identical light chains (23 kD) held together by interchain disulfide bonds and by noncovalent interactions (Sutton et al., 2019).

IgE’s main function is immunity to parasites such as helminths like Schistosoma mansoni, Trichinella spiralis, and Fasciola hepatica. IgE is utilized during immune defense against certain protozoan parasites such as Plasmodium falciparum. IgE may have evolved as a last line of defense to protect against venoms. IgE also has an essential role in type I hypersensitivity, which manifests in various allergic diseases, such as allergic asthma, most types of sinusitis, allergic rhinitis, food allergies, and specific types of chronic urticaria and atopic dermatitis. IgE primes the IgE-mediated allergic response by binding to Fc receptors found on the surface of mast cells and basophils. Fc receptors are also found on eosinophils, monocytes, macrophages and platelets in humans. There are two types of Fcε receptors FcεRI (type I Fcε receptor), the high-affinity IgE receptor and FcεRII (type II Fcε receptor), also known as CD23, the low-affinity IgE receptor. IgE may play an important role in the immune system’s recognition of cancer (Luker et al., 2019).

To advance related research and diagnostics, recombinant antibody technology has been used to develop highly reproducible IgE proteins in a wide range of species. These Fc-only proteins can be used for a variety of applications including assay standards to create reproducible control sera by spiking the IgE into normal sera. They can be used as immunogens to generate antibodies against the immunoglobulin Fc domain and be engineered into antigen-specific antibodies, to make an IgE antibody for your allergy or autoimmunity research. We offer IgE Fc domain proteins in a variety of species, including human, mouse, dog, cat and horse. These proteins are ideal for veterinary research and diagnostic assay design.

References

  • Luker et al. A new look at IgE beyond allergies. Version 1. F1000Res. 2019; 8: F1000 Faculty Rev-736.
  • Sutton et al. IgE Antibodies: From Structure to Function and Clinical Translation. Antibodies (Basel). 2019 Mar; 8(1): 19.

Veterinary IgE Fc Proteins

We are pleased to offer IgE Fc domain proteins in a variety of species, including human, mouse, cat, dog and horse. These IgE Fc domain proteins react with species-specific anti-IgE antibodies, with no observed cross-reactivity.
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