There is no product in the shopping cart, buy it!
Glycoprotein detection is an important part of glycosylation engineering. Combining first-in-class technologies with experienced technical team, Creative Biolabs has successfully developed a high-sensitive glycoprotein detection platform to offer the most diverse portfolio of glycoprotein detection products and services. The values of quality, timing and price is our basic criterion. We will try our best to help you get milestone success in your glycoprotein project.
As a common co-/post-translational modification, glycosylation plays profound effects on protein structure and function. Many biologically interesting proteins, such as vaccines, antibodies, and enzymes, are glycosylated at their asparagine, serine, and threonine residues. Glycoproteins have been shown to associate with increasing applications in therapeutics, such as plasminogen activator for the treatment of myocardial infarction and strokes, erythropoietin for anemia and various monoclonal antibody-based treatments for cancer. But the complexity of the glycan structures, the multiple substitutions (microheterogeneity) at glycosylation sites, and the structural diversity associated with the protein backbone itself makes the glycoprotein analysis becomes an enormous task. The key effects that glycoproteins have on biological processes and clinical applications stimulate the development of detection and analytical strategies with increasing sensitivity and throughput.
In order to perform reliable, detailed detection of glycoproteins, we provide a series of technologies for glycoprotein detection and analysis. Staining and affinity-based methods are two generally used methods.
Glycoprotein gel-staining is one of the simplest ways to estimate whether a protein is glycosylated. During the staining procedures, sugar groups of glycoproteins are often chemically restructured with periodic acid to overcome the problem that glycan sugar moieties are not reactive to staining or labeling molecules. The periodic acid oxidizes vicinal hydroxyls on sugars (especially sialic acid) to aldehydes or ketones, which reacts with the Schiff reagent to give a magenta color. This periodic acid-Schiff (PAS) stain can be used to detect and quantify glycoproteins in various biological samples. Notably, it can also be used to make sugars reactive towards crosslinkers, which can be covalently bound to labeling molecules (e.g., biotin) or immobilized support (e.g., streptavidin) for detection or purification.
The affinity-based glycoprotein detection is widely used and facilitate the determination of the glycosylation type. According to the different molecules that glycoprotein combined, affinity-based detection can be classified into three types, namely saccharide-binding proteins, enzyme-based methods, and antibody-based methods. These biomolecules have been used to label and isolate glycosylated proteins containing a specific sugar (such as O-GlcNAc or mannosamine) with high specificity and efficiency. The glycan-specific antibodies can specifically recognize the specific sugar on a given protein. Moreover, our glycoprotein labeling kits can tag sugars with fluorescent moieties, which is convenient for direct detection or improved mass spectrometric (MS) ionization.
Fig.1 Schematic view of glycoproteomics methods for glycoproteins and glycopeptides (Nilsson, 2013).
With decades of experience, Creative Biolabs has successfully completed a lot of glycoprotein detection projects. We are committed to applying high-quality products, services, and communications to meet your specific project needs. Our off-the-shelf product portfolio and services can help you get landmark development. If you are interested, please contact us without hesitation.
Reference