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IgA Glycosylation Service

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Creative Biolabs has extensive experience in offering multiple glycosylated antibody development services for both therapeutic and laboratory applications. Relying on our cutting-edge technology platform, we are confident in accelerating the development of global customers' projects. Here, we are happy to introduce our high-quality IgA antibody glycosylation service.

Introduction of IgA Glycosylation

Antibody glycosylation is a common and important post-translational modification that impacts the stability, biological functions and clearance of antibodies. Using glycoengineering to produce antibodies with specific glycoforms is beneficial to improving therapeutic efficacy. Generally, there are two main classes of glycans for antibodies, namely the N-linked glycans (linked to a nitrogen atom, or N) and the O-linked glycans (linked to an oxygen atom, or O). The N-glycans can be found at the asparagine in a known consensus sequence, whereas O-linked glycans can be linked to serine or threonine residues, generally in a proline-rich region. Compared to IgG, IgA antibodies possess a more complex N-glycosylation because of better accessibility of the glycans for glycosyltransferases within the Golgi. Furthermore, compared with one N-glycosylation site of IgG antibodies, IgA1 antibodies have two conserved N-glycosylation sites and O-glycosylation in the hinge region, while IgA2 sub-isotypes have two or three additional N-glycosylation sites.

Schematic representation of immunoglobulin A (IgA) and IgG and their respective glycosylation sites can be detected by glycopeptide analysis of serum-derived samples.Fig.1 Schematic representation of immunoglobulin A (IgA) and IgG and their respective glycosylation sites can be detected by glycopeptide analysis of serum-derived samples. (Bondt, 2017)

IgA Glycosylation Services Provided by Creative Biolabs

Post-translational glycosylation is important for antibody's function, bioavailability, immunogenicity and clearance, even for pharmacokinetics and pharmacodynamics (PK/PD) in the therapeutic antibodies used for diseases treatment. During the past years, several expression systems have been developed for the production of recombinant IgA antibodies, including but not limited to myeloma cells, monkey-derived COS cells, insect cells, baby hamster kidney cells, and plants. And most of the recombinantly-produced IgA antibodies were expressed in Chinese hamster ovary (CHO) cells. However, non-human glycan structures attached to these therapeutic antibodies may result in immunological reactions, so it requires the modification of glycosylated engineering. Based on advanced technology and professional scientists, Creative Biolabs is able to optimize the glycosylation of these therapeutic non-IgG antibodies by using our human glycol-engineered cells systems to decrease side effects and improve clinical efficacy. In addition, we can also help worldwide customers to evaluate predominant glycan structures by N-glycosylation profiles analysis of these recombinant IgA antibodies.

IgA1 glycosylation sites.Fig.2 IgA1 glycosylation sites. (Amore, 2001)

Features of Our Services

  • Higher productivity: fast generation of high-yield monoclonal IgA antibody-producing clones
  • Better quality of the produced molecules with respect to more completely processed N-glycans
  • Higher reproducibility and full scalability from 10 mL-1000 L bioreactors
  • Best after-sale service and professional technical assistance

With vast experience and enthusiasm in glycosylated antibody development, Creative Biolabs has always been devoted to delivering best-in-class services to our worldwide customers. Our scientists are happy to discuss with you to tailor the most appropriate plan for your project. If you are interested in the services we provide, please feel free to contact us for more details.

References

  1. Bondt, A.; et al. IgA N- and O-glycosylation profiling reveals no association with the pregnancy-related improvement in rheumatoid arthritis. Arthritis Research & Therapy. 2017, 19: 160.
  2. Amore, A.; et al. Glycosylation of circulating IgA in patients with IgA nephropathy modulates proliferation and apoptosis of mesangial cells. Journal of the American Society of Nephrology. 2001, 1862-1871.

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