Anguilla anguilla lectin (AAL), binds not only polysaccharides containing L-fucose and D-galactose methylether derivatives but also recognizes the H and Lea antigens. The structure of the AAL-fucose complex reveals the architecture of the physiological trimer and allows the identification of the interactions that define the specificity of animal fucose-binding lectins and several related proteins. Therefore, extraction and analysis of AAL is beneficial for glycobiology. CD BioGlyco offers clients a full range of Lectin Production Services, we are committed to being your best partner in the field of glycobiology.
Blood samples are collected from anesthetized Anguilla anguilla by venipuncture. Separate the serum by centrifugation after clotting at room temperature.
The liver and intestine are excised from the Anguilla anguilla and immediately placed in liquid nitrogen for preservation. Tissue is ground to a powdered state under liquid nitrogen conditions. Add the buffer solution, and centrifugation to collect the supernatant.
We use two-step chromatography to isolate the AAL. The first step uses an agarose affinity chromatography column purification, and collection fraction absorbance detection. The second step uses high-performance liquid chromatography (HPLC) size exclusion chromatography. The purification conditions have been optimized countless times.
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Title: A novel fucose recognition fold involved in innate immunity
Journal: Nature Structural & Molecular Biology
IF: 18.361
Published: 2002
Background: Anguilla anguilla agglutinin (AAA) is a mucin extracted from European eel serum. It is involved in the recognition of bacterial lipoglycans by the animal's innate immune system. In AAA analysis, a newly discovered carbohydrate recognition domain was identified. Therefore, it is essential to analyze the biological and functional roles of AAA as comprehensively as possible.
Research Findings: The crystal structure of the AAA defines the fold of this type of fucose-specific lectin. It provides the basis for understanding its α-L-fucose specificity and allows the identification of this fold and prediction of functions in many other proteins or protein domains of organisms ranging from bacteria to animals. The diversity of primary structures that share a similar tertiary structure suggests either convergent evolution or a high tolerance for mutations in this fold. Finally, the ubiquity of this fold warrants the use of the F-lectin or F-type lectin fold as a common name for members of this lectin family.
Fig.1 The structure and model of the interactions AAL. (Bianchet, et al., 2002)
CD BioGlyco has many years of successful experience in the field of glycobiology. We have achieved perfect cooperation with clients in many countries. We offer a wide range of Animal Lectin Production services. Please feel free to contact us if you have any needs in AAL.
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