Recombinant Sialic Acid Binding Proteins

Recombinant Sialic Acid Binding Proteins

Many recombinant proteins are used to analyze specific sialic acids, sialylglycans, and their modifications on cells or tissues. CD BioGlyco has been committed to sialic acid research for many years, and we provide high-quality sialic acid analysis services for cells and tissue samples using recombinant sialic acid-binding proteins.

The Role of Sialic Acids

Sialic acids, usually located on the terminal branches of N-glycans, O-glycans, and glycosphingolipids, are one of the most complex and versatile molecules in life. Because of its important role in cellular recognition and signaling, sialic acids serve as a key element in the sugar epitope of cells and lectins. During pathological processes, sialic acids act as a binding site for various pathogens and toxins. Sialic acids also act as a ligand for glycan-binding proteins such as animal lectins, viral lectins, and bacterial lectins. Microbial pathogens evade the host immune response by "molecular mimicry" binding host sialic acids.

Sialic acids on cell surface.Fig.1 Sialic acids on the cell surface. (Wasik, 2016)

Recombinant Sialic Acid Binding Proteins

Sialic acid is recognized by many endogenous and exogenous specific binding proteins in biological processes. Therefore, many recombinant proteins, such as sialic acid-specific recombinant microproteins, recombinant sialic acid-binding immunoglobulin-like lectins (Siglecs)-fragment crystallizable (Fc) fusion proteins, and recombinant endoenuraminidase-green fluorescent protein (GFP) fusion proteins, are used to analyze specific sialic acids, sialic acid glycans and their modifications on cells or tissues. For example, heterologously expressed ectodomain of recombinant influenza C virus hemagglutinin esterase has proven to be a useful tool for studying the biological distribution and functions of 9-O-acetylated sialic acid.

Differential expression of O-acetylated sialic acids in cells and tissues detected by lectin immunofluorescence assay.Fig.2 Differential expression of O-acetylated sialic acids in cells and tissues detected by lectin immunofluorescence assay. (Zhang, 2018)

Our Services

Recombinant sialic acid-binding proteins are powerful tools to analyze specific sialic acids, sialyl glycans, and their modifications on cells or tissues. CD BioGlyco provides high-quality sialic acid analysis services using recombinant sialic acid-binding proteins for our clients. Our recombinant proteins are as follows:

  • Sialic acid-specific recombinant microbial proteins

Sialic acid-specific recombinant microbial proteins are powerful tools to detect specific sialic acids on cells and tissues. We analyze 9-O-acetylated sialic acid on the cell surface by the recombinant influenza C virus hemagglutinin esterase. Moreover, we also distinguish between several closely related O-acetylated sialic acids by dual-functional nidoviruses hemagglutinin esterase envelope protein.

  • Recombinant Siglec-Fc fusion proteins

Siglecs are members of the Ig superfamily that recognize sialic acid residues in glycoproteins. We also detect cell surface sialic acids by recombinant Siglec protein such as Siglec-E:Fc, Siglec-F:Fc, and Siglec-2:Fc.

  • Recombinant endoenuraminidase-GFP fusion proteins

We use recombinant endoenuraminidase-GFP fusion proteins as molecular beacons to detect polysialic acid on the cell surface by fluorescence microscopy, binding assay, and immunoblotting.

Advantages of Us

  • Multiple recombinant proteins
  • Personalized analytics solutions
  • Experienced scientists
  • Complete data and analysis report

CD BioGlyco has developed a complete set of Strategies for Sialic Acid Analysis. We provide accurate, simple, and rapid sialic acid analysis services for our clients worldwide. If you are interested in our analysis strategy using recombinant sialic acid-binding proteins, please feel free to contact us for more information.

References:

  1. Wasik, B.R.; et al. Effects of sialic acid modifications on virus binding and infection. Trends in microbiology. 2016, 24(12): 991-1001.
  2. Zhang, X.; et al. Recent approaches for directly profiling cell surface sialoform. Glycobiology. 2018, 28(12): 910-924.
This service is for Research Use Only, not intended for any clinical use.

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