Fostering Innovation through Halichondria okadai Lectin Expertise
Sponges are a group of multicellular animals whose genetic diversity allows them to express various types of molecules such as monosaccharides, polysaccharides, or lectins. Lectins from Marine Sponges have important characteristics compared to plant lectins, such as low immunogenicity and the ability to bind complex glycans. CD BioGlyco has a top-level Marine Biomolecule research team dedicated to the production of Marine Source Lectins.
Here we provide one one-stop solution for extraction, purification, and characterization of lectins from sponge Halichondria okadai.
Extraction of lectins
A neutral buffer is added to pulverized Halichondria okadai for extraction followed by high-speed centrifugation. The supernatant is taken dialyzed and dried to obtain the crude lectin.
Purification of lectins
We offer several Purification Techniques to purify Halichondria okadai lectin. Examples include the following:
- Affinity chromatography: Purification of lectins using differences in the strength of interactions between different biomolecules between the lectin, the impurity, and the stationary phase. The stationary phase is usually a gel matrix, commonly agarose.
- High-performance liquid chromatography (HPLC): HPLC is the most commonly used chromatographic technique for separating lectins and other small molecules and determining their purity.
- Gas chromatography (GC): GC can be used to separate volatile impurities from lectins to purify them.
Characterization of lectins
We offer Fourier transform infrared spectroscopy (FTIR), GC-mass spectrometry (GC-MS), and nuclear magnetic resonance (NMR) to identify and characterize the multilevel structure of lectins.
Atomic force microscopy (AFM) and scanning electron microscopy (SEM) can be used to research the surface structure and properties of lectins.
- Molecular weight analysis
Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and gel permeation chromatography (GPC) are two effective methods for determining the molecular weight of lectins.
- Analysis of haemagglutination activity
We add lectin solution, buffer solution, and blood erythrocytes to the haemagglutination plate, observe the results with the naked eye or microscope, and record the maximum dilution at which the lectin shows a coagulation reaction.
Publication Data
Technology: Affinity chromatography and GPC
Journal: Toxins
IF: 4.2
Published: 2012
Results: In this article, the authors used affinity chromatography to isolate a tetrameric lectin from the sponge Halichondria okadai, which consists of four non-covalently bound 18 kDa subunits, and is stable at pH 4-12 and temperatures below 60°C. The lectin was found to be highly inhibitory to the haemagglutination activity of the sponge Halichondria okadai. The haemagglutinating activity of the lectin was strongly inhibited by chitosan, fetuin, and mucin from the porcine stomach and bovine submandibular gland. In addition, the lectin kills leukemia cells and K562 erythroleukaemia cells in a carbohydrate-dependent manner.
Fig.1 GPC (A) and molecular weight calibration curve (B) of Halichondria okadai lectin. (Matsumoto, et al., 2012)
Applications
- Halichondria okadai lectin plays an important role in innate immunity and the development of the animal's body size, so it can be used in research on the growth and development of marine animals.
- Halichondria okadai lectin has anti-tumor properties and can be used in the development of anti-tumor drugs.
- Halichondria okadai lectin can be used as a probe for cell surface glycans in cell biology.
Advantages
- Our research team has advanced biomolecule production techniques to provide our clients with consistently high-quality Halichondria okadai lectin.
- We offer many types of isolation and purification techniques to obtain Halichondria okadai lectin of high purity and biological activity.
- We have extensive knowledge of lectin properties and structure and use this knowledge to provide superior Halichondria okadai lectin products.
Frequently Asked Questions
Why do we produce marine lectins?
Marine-derived lectins are glycoproteins or glycoconjugated peptides found in marine organisms that promote cell recognition and adhesion, and some also exhibit anti-inflammatory biological activities. Compared to terrestrial lectins, marine-derived lectins tend to exist as monomers, are structurally simpler, and have a wide range of biological activities.
What role does sponge-derived lectin play in organisms?
Sponge-derived lectin exerts a variety of immunomodulatory functions, including pathogen recognition, inflammation, participation in various blood cell functions (e.g., agglutination), phagocytosis, etc. Sponge-derived lectin also controls cell proliferation, protein folding, RNA splicing, and molecular transport. In addition, sponge-derived lectin has a good inhibitory effect on acute infection of human T-lymphocyte cell lines.
CD BioGlyco is a leading biology company with extensive knowledge of the nature and structure of marine lectins. With our expertise in lectin production, we help our clients explore Halichondria okadai lectin and reveal their functions in biological systems. If you are interested in our services, please feel free to contact us and work together on marine lectin research.
Reference
- Matsumoto, R.; et al. Cytotoxicity and glycan-binding properties of an 18 kDa lectin isolated from the marine sponge Halichondria okadai. Toxins. 2012, 4(5): 323-338.
