Limulus Polyphemus Lectin Production Service
L. polyphemus lectin is a highly specific lectin, whose specific ligand is neuraminic acid. Its agglutination and mitotic process are influenced by glycans containing sialic acid. Its main activity shows agglutination on horse red blood cells, white mouse red blood cells, and human red blood cells. Therefore, it is important to produce and analyze L. polyphemus-derived lectins and assess the relationship of their structure with sugar-specific proteins. Our professional talents combined with strong biological background knowledge provide clients with high-quality extraction, isolation, and purification services.
L. polyphemus Lectin Extraction Service at CD BioGlyco
- Collection of hemolymph: Under the conditions of negative pressure, we draw blood by inserting the anesthetized L. polyphemus with a needle into the chest and abdomen. No anticoagulant is added to low-temperature centrifugation. Take the blue supernatant and discard the precipitate.
- Isolation of serum: Our company pays extra attention to the quality of the extracts. We centrifuge the serum three times at low temperatures for long periods, collecting only the supernatant each time. The collected supernatant needs to be cryo-dialyzed for 24 hours.
L. polyphemus Lectin Purification Service at CD BioGlyco
At CD BioGlyco, we provide DEAE-Sephadex and affinity gel filtration chromatography separation services. In the first step, DEAE-Sephadex column chromatography is used to remove some of the impurities; in the second step, affinity chromatography to purification. Bovine mandibular mucin replacement of the original substrate substitution in buffer containing CaCl2, some impurities are eluted by increasing ionic strength, and pure lectin is eluted with calcium-free buffer. Our company provides comprehensive Lectin Production Services to meet the needs of clients from small scale to large scale.
L. polyphemus Lectin Analysis Service at CD BioGlyco
- Determination of protein content: Folin-phenol reagent quantification.
- N-terminal amino acid sequence analysis: We provide protein sequencing, gas chromatography-mass spectrometry (GC-MS) analysis, in silico thin layer chromatography, and amino acid analysis.
- Purity determination: The purity of the preparation is determined by polyacryphthalide gel electrophoresis.
- Vitality measurement: The agglutination results are observed with a microscope, and the intensity of the agglutination reaction is judged by the degree of cell dispersion or condensation.
- Others: We provide cell culture services such as Hela and Caco2. Moreover, we offer animal experiment services such as mice or rabbits. Our technicians follow the whole process.
Fig.1 Schematic diagram of L. polyphemus lectin production service. (CD BioGlyco)
Applications of L. polyphemus Lectin
- L. polyphemus lectin is used to detect small changes in the surface chemistry that accompany cell transformation.
- L. polyphemus lectin serves as a biochemical reagent to provide useful tools for studying the structure and function of sugars and complex sugars.
- L. polyphemus lectin has some anti-inflammatory activity, and it has a good agglutination effect on platelets.
Advantages of Us
- Three fractions are obtained by affinity chromatography. The first two components (Limulin I and II) do not condense red blood cells, but the third component (Limulin III) is very active.
- Optimized purification process for effective removal of impurities and better isolation of lectins.
CD BioGlyco attaches great importance to the production of Natural Lectin. Isolations are extracted without disrupting the lectin structure. Our company has accumulated a lot of experience in the production of Animal Lectin. Please feel free to contact us if you are interested in our services.
References
- Finstad, C.L.; et al. The erythrocyte agglutinin from Limulus polyphemus hemolymph: molecular structure and biological function. Ann N Y Acad Sci. 1974, 234(0): 170-82.
- Roche, A.C.; et al. Circular dichroism of limulin: Limulus polyphemus lectin. FEBS Lett. 1978, 91(2): 233-6.
- Roche, A.C.; et al. Protein-sugar interactions. Purification by affinity chromatography of limulin, an N-acyl-neuraminidyl-binding protein. FEBS Lett. 1975, 57(3): 245-9.
This service is for Research Use Only, not intended for any clinical use.