Holothuria scabra lectin (HSL) is a monomeric glycoprotein with a molecular weight of 182 kDa, stable under high temperature and pH. The hemagglutination activity of HSL does not require any divalent metal separation. HSL binds to dealkyl glycoproteins, T antigen, and T (α-ser) antigens and distinguishes β-1,4 and β-1,3 junctions. Detailed exploration of the phagocytic and opsonization effects of HSL in innate immunity may help to develop broader applications.
Collect adult H. scabra and store them in circulating seawater for a few days. Ambient humidity and seawater salinity are similar to the collection site.
Dissection of sea cucumber and collection of coelomic fluid. Centrifuge to remove coelomocytes, treat with serine protease inhibitors, and store at -20°C. It is important to note that the anticoagulant is added immediately after extraction.
Firstly, the removal of small molecule contaminants from coelomic fluid using ultrafiltration membranes. Heat treatment for 2 h at 60°C to inactivate the protease. Then, add Tris-HCl buffer and solid ammonium sulfate to bring the concentration to a constant value. Finally, the overcolumn treatment is performed.
For the purification columns, we use phenyl agarose columns with hydrophobic interactions. For the first eluted lectin fractions, mix them, add ammonium sulfate, change the concentration, and run the column a second time. Elute with buffer, collect target fractions, and store at 4°C.
Based on purified HSL, we offer a wide range of analytical services, from basic protein content determination to activity analysis. We support our clients to provide purified lectins for analytical, all you need to do is to give us your samples.
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Fig. 1 Schematic diagram of HSL analysis service. (CD BioGlyco)
Paper Title: Purification and characterization of a T-antigen specific lectin from the coelomic fluid of a marine invertebrate, sea cucumber (Holothuria scabra)
Journal: Fish&Shellfish Immunology
IF: 4.622
Published: 2008
Results: H. scabra produces a high molecular weight monomeric glycoprotein with t-antigen specificity. The hemagglutinating properties of HSL are unique because it does not require any divalent metal ions. The hemagglutination activity was inhibited by MeaGal, t-antigen, and deacyl glycoprotein.
Fig.2 Chart of analyzed data of HSL. (Nagaraji, et al., 2008)
CD BioGlyco has been serving in Animal Lectin Production for many years. Our professional technicians have accumulated a wealth of successful experience. We have comprehensive extraction and purification analysis process services, to meet the full range of clients' needs. Please feel free to contact us.
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