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Therapeutic IgA Antibody Discovery

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Creative Biolabs is a forward-looking company as well as a leading customer service provider in the field of IgA antibody development. Our scientists specialized in therapeutic antibody studies will work with you to develop the most appropriate strategy that will offer the most meaningful data for your research. We have experienced experts and advanced platforms that are able to provide excellent discovery services on therapeutic IgA antibodies.

Introduction to IgA Antibodies

IgA antibody, the second most important antibodies in the serum, is responsible for activating the complement pathway and immune system. IgA is a multivalent antibody that is easily identified on the surface of the mucosa. Most of the secreted IgA can be identified on the surface of the mucous membrane, such as the respiratory tract, digestive tract, urogenital tract, and thereby protect the intestine from pathogens while maintaining the homeostasis of the intestine. Meanwhile, recent studies have demonstrated that the lgA can neutralize a number of pathogens by different mechanisms and then trigger defense against various infections.

In general, IgA antibodies are made up of two heavy chains and two light chains. Each chain consists of a constant region, a hinge region as well as a variable region. Furthermore, the total molecular weight of the IgA antibody is about 160 kDa. IgA isotype antibody is prone to be in monomeric form in human serum while in dimeric and secretory forms at the mucosal site. The unique 18-amino acid tail of IgA antibody is a key factor in oligomerization. IgA is comprised of two subtypes, IgA1 and IgA2, and can bind to several receptors, such as FcαRI (CD89), polymeric Ig-receptor (pIgR), asialoglycoprotein, Fcα/μR, as well as transferrin.

 Schematic illustration of IgG1 and IgA antibodies.Fig.1 Schematic illustration of IgG1 and IgA antibodies. (Hart, 2017)

Therapeutic Effects of IgA Antibodies

Recent researchers have revealed that the IgA antibody can be considered as a potential therapeutic tool on a number of disease treatments, particularly cancers and immune diseases. The secreted IgA (sIgA) in the background of the mucous membrane can produce a variety of secretory components (SCs) and then cover the Fc region of IgA, providing protection against protein hydrolysis damage. Besides, IgA can bind to FcαRI in neutrophils and a range of cytotoxic immune cells, leading to neutrophil and/or monocyte-dependent phagocytosis. Moreover, many investigations conducted on IgA antibodies have shown that IgA antibodies can improve signaling transduction on a panel of tumor cells, and can be actively transported to mucosal secretions, which may improve the targeting of certain cancers. Therefore, numerous IgA antibodies have been developed by recombinant DNA technology and widely used in cancer therapy. In our company, we have generated a series of IgA antibodies against targets for a wide variety of diseases, such as anti-(HER2/neu x FcαRI) BsAb, anti-Her2 IgA2 antibody, anti-EpCAM IgA monoclonal antibody, anti-CD20 IgA2 antibody, as well as anti-EGFR IgA2 antibodies for liquid and solid tumors treatment.

 Therapeutic potential of IgA monoclonal antibodies.Fig.2 Therapeutic potential of IgA monoclonal antibodies. (Bakema, 2011)

Creative Biolabs is a leading global biotech company which provides a series of antibody development solutions for worldwide customers. With our proven competencies and regulatory expertise, we are therefore confident in offering the best non-lgG therapeutic antibodies products. More importantly, related non-IgG antibodies services and applications are also within our line of business and capabilities based on our powerful technology platform.

If you are interested in our services, please contact us for more details.

References

  1. Hart, F., et al. Human Cell Line-Derived Monoclonal IgA Antibodies for Cancer Immunotherapy. Bioengineering (Basel). 2017, 8: 4(2).
  2. Bakema, J.E.; van Egmond, M. Immunoglobulin A: A next generation of therapeutic antibodies? mAbs. 2011, 3(4): 352-361.

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