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Lectin-Fc Chimeras for Glyco-code Based Diagnostics

Lectin-Fc chimeras are one of the most important tools in exploring glyco-code based diagnostics. With rich experience and professional foundations, Creative Biolabs is confident in offering quality-guaranteed Lectin-Fc chimera development services to help our customers accelerate their researches for glyco-code based diagnostics.

Overview of Glycan in Diagnostics

Glycosylation is the most common form of co-translational and post-translational modification, with as many as 70% of all human proteins estimated to contain one or more glycan chains, and it is an enzyme-directed site-specific process, which is also critical for a wide range of biological processes, including cell attachment to the extracellular matrix and protein-ligand interactions in the cell. A number of different types of human protein glycosylation exist, including N-linked to Asn, several types of O-linked to Ser, Thr, hydroxylysine, and Tyr residues, and C-mannosylation to Trp and the glycans attached to proteins exhibit tremendous structural variation. Glycans biosynthesis is markedly influenced by disease states and glycosylation can potentially affect nearly every glycoprotein produced in the diseased as well as act as a key regulatory mechanism controlling several physiopathological processes. Therefore, the effect of the disease state on the biosynthesis of glycans may be more evident than that of disease-related biomolecules changes. Altered glycosylation of tumor cells often occurs in the early stages of tumor development, and certain tumor-associated glycans are expressed in precursor lesions of different types of cancer, making them powerful early diagnostic markers.

Glycosylation changes in cancer that connect to immune recognition. Fig.1 Glycosylation changes in cancer that connect to immune recognition. (RodrIguez, 2018)

Lectin-Fc Chimeras

Most carbohydrates are T-cell independent antigens with low antigenicity, and frequently induce low antibody titers, which impairs mAbs production. Thus in the past two decades, one of the main ways to investigate glycosylation was by using lectins. Lectins are naturally occurring substances, most derived from plant or sometimes invertebrate sources, which are carbohydrate-binding proteins that may interact with high specificity to a soluble carbohydrate or to a carbohydrate moiety that is a part of a glycoprotein or glycolipids. An interesting alternative is the construction of fusion proteins composed of lectins, natural carbohydrate ligands, directly linked to the Fc domain of immunoglobulin (Ig), replacing its binding arms and promoting specific recognition of fungal antigens.

Lectin-Fc Chimeras in Research

Penaeus monodon PmAV has anti-viral activity. Litopenaeus vannamei LvLT with two CRDs may play a role in white spot syndrome virus (WSSV) infection, F. chinensis Fc-hsL, which has a single CRD, is specifically expressed in hepatopancreas and exhibits antimicrobial activity. F. chinensis Fclectin, which has two CRDs, is expressed in hemocytes and is up-regulated upon challenge with WSSV. Researchers developed a novel C-type lectin with two dissimilar CRDs from the Chinese shrimp F. chinensis. This new lectin, designated Fc-Lec2, was constitutively expressed in the hepatopancreas, and its expression was greatly up-regulated upon bacteria and WSSV challenge. Recombinant Fc-Lec2 and its CRD1 and CRD2 proteins were produced. Fc-Lec2 bound to several microorganisms, including Gram-positive and Gram-negative bacteria and yeast, in the absence of Ca2+, but agglutinated these bacteria in a Ca2+- dependent manner. Fc-Lec2 appeared to have broader specificity to agglutinate bacteria and a higher affinity to bind bacteria than its individual CRD1 or CRD2.

Services at Creative Biolabs

Exploration of glyco-code in diagnostics has attracted the sights of researchers. Creative Biolabs has never stopped our steps in pursuing the frontage of science. We have established a comprehensive technology platform for glyco-code based diagnostics. Our platform offers various high-quality technologies services including lectin–Fc chimeras development services for glyco-code based diagnostics. Besides, we also help with tumor-associated glycan detection services including but are not limited to:

If you are interested in any one of our services, or you have questions during your glycoprotein researches, please feel free to contact us for more information.

Reference

  1. RodrIguez, E.; et al. The tumor glyco-code as a novel immune checkpoint for immunotherapy. Nat Rev Immunol. 2018, 18(3): 204-211.
For Research Use Only.

Related Services:

  1. ELISA for Glyco-code Based Diagnostics
  2. Lectin Blot Analysis for Glyco-code Based Diagnostics
  3. RNA Sequencing for Glyco-code Based Diagnostics
  4. RNA Microarray for Glyco-code Based Diagnostics
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