Empowering Research with Halicondria panacea Lectin Production Excellence
Sponges are multicellular and porous lower marine animals and are one of the most important sources of Marine Biomolecule. Proteins from sponges have good biological activities such as erythrocyte agglutination activity, inhibition of enzyme activity, and promotion of mitosis. Since lectins are carbohydrate-binding proteins, Lectins from Sponges are also biologically active.
Here at CD BioGlyco, with our highly skilled Marine Lectin production and purification technology, we offer high-quality sponge Halicondria panacea lectin production services to our clients.
Extraction of Halicondria panacea lectin
The sponge Halicondria panacea is crushed and the appropriate amount of deionized water is added, followed by centrifugation of the sponge, collection of the supernatant, and freeze-drying to obtain a crude lectin with insoluble matter removed.
The crude lectin is dissolved in a buffer solution and the process is continued by centrifugation. The supernatant is then collected and ethanol is added to it and the lectin appears as a precipitate. Finally, the precipitate is freeze-dried to obtain a relatively pure Halicondria panacea lectin.
Purification of Halicondria panacea lectin
Halicondria panacea lectin is a macromolecule substance, we use gel chromatography combined with cellulose ion exchange chromatography to purify it.
- Gel chromatography: The lectin sample to be purified is dissolved with buffer, then added to the gel column and eluted with buffer, the eluate is collected according to the signal value of the peaks and concentrated.
- Cellulose ion exchange chromatography: The eluate obtained in the previous step is concentrated and added to the cellulose ion exchange chromatography column, eluted by gradient elution, the components at specific wavelengths are collected, and the pure Halicondria panacea lectin can be obtained by freeze-drying.
After purification, we detect the purity of Halicondria panacea lectin by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
Analysis of Halicondria panacea lectin
- Structural characterization: We offer a comprehensive range of Halicondria panacea lectin structural characterization services as shown in Table 1.
Table 1 Structural characterization of Halicondria panacea lectin.
|
Structural information |
Methods |
| Glycosyl composition and proportions |
Acid degradation, paper chromatography (PC), gas chromatography (GC), liquid chromatography (LC) |
| Glycan chain carbon configuration |
Infrared spectroscopy (IR), nuclear magnetic resonance (NMR) |
| Glycan chain linkage order |
Acid hydrolysis, enzymatic hydrolysis |
| Hydroxyl substitution |
GC, NMR, mass spectrometry (MS) |
- Molecular weight assay: We offer gel filtration and MS to detect molecular weight and subunit molecular weight of Halicondria panacea lectin.
- Agglutination activity analysis: We analyze the agglutination activity of Halicondria panacea lectin using the erythrocyte agglutination test. Saline, diluted Halicondria panacea lectin, and erythrocyte suspension are added gradually to the wells of the agglutination plate, and the precipitation state of the erythrocytes is observed under a microscope or the naked eye to detect the agglutination activity of Halicondria panacea lectin.
Applications
- Lectins are a class of glycoproteins that recognize and bind to specific monosaccharides or glycan structures, thus Halicondria panacea lectin can be used in the isolation and purification of oligosaccharides or glycoconjugates and research on the analysis of glycan structures.
- Halicondria panacea lectin can bind to cell surface glycans, thus Halicondria panacea lectin can be used to promote cell recognition and adhesion.
- Halicondria panacea lectin can be used in research on the regulation of the body's immune system, inflammatory response, and activation of inflammatory cells.
Advantages
- Our sponge lectin production team possesses first-class lectin production technology and provides a one-stop Halicondria panacea lectin production solution for extracting, purifying, and analyzing.
- Our Halicondria panacea lectin production services are characterized by high efficiency and high quality and can be widely used in pharmaceuticals, nutraceuticals, and biotechnology.
- Sponge ecosystems are part of marine biodiversity, and we promote the sustainable use and development of marine resources through the rational development and use of sponge lectins.
Frequently Asked Questions
What are the biological activities of marine sponge lectins?
- Coagulation: Marine sponge agglutinin can bind suspended substances or microorganisms in the water to form large aggregates, thus prompting these particles to settle to the bottom of the ocean and purify the ocean of pollutants.
- Antibacterial activity: Marine sponge lectins have certain inhibitory effects on microorganisms such as bacteria, fungi, and viruses, and have certain antibacterial activity.
- Anti-blood clotting activity: Some marine sponge lectins have anti-blood clotting activity and can be used to treat cardiovascular disease or reduce the risk of thrombosis.
- Antioxidant activity: Some marine sponge lectins have antioxidant activity, which helps scavenge free radicals in the body and reduce the damage caused by oxidative stress.
What methods of glycan structure analysis can be developed from lectins?
The methods for glycan structure analysis of glycoproteins using lectins include lectin precipitation, lectin affinity chromatography, lectin affinity electrophoresis, lectin enzyme-linked immunosorbent assay, and lectin blotting.
CD BioGlyco has a team of specialized marine biomolecule researchers dedicated to the production of various types of lectins from marine organisms. We offer custom Halicondria panacea lectin production solutions and lectin products according to our client's needs. Please feel free to contact us to explore the mysteries of marine glycobiology.
Reference
- Gomes Filho, S.M.; et al. Marine sponge lectins: actual status on properties and biological activities. Molecules. 2015, 20(1): 348-357.
