SNA is isolated from the inner bark (bast tissue) of elder stems and branches. The lectin is not blood group specific but has an affinity for α-NeuNAc-[2→6]-Gal, α-NeuNAc-[2→6]-GalNAc, and, to a lesser extent, α-NeuNAc-[2→3]-Gal residues.
Packaging
Package size based on protein content
Physical form
Lyophilized powder containing NaCl
Preparation Note
Affinity purified by a modification of Broekaert.[1]
Analysis Note
Agglutination activity is expressed in μg/ml and is determined from serial dilutions in phosphate buffered saline, pH 7.3, of a 1 mg/ml solution. The activity is the lowest concentration to agglutinate a 2% suspension of human blood group A erythrocytes after 1 hr incubation at 25 °C.
The Biochemical journal, 221(1), 163-169 (1984-07-01)
A lectin was isolated from elder (Sambucus nigra) bark by affinity chromatography on fetuin-agarose. It is a tetrameric molecule (Mr 140000) composed of two different subunits of Mr 34500 and 37500 respectively, held together by intramolecular disulphide bridges. The lectin
Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, 33(7), 930-935 (2003-07-16)
Atopy is closely associated with the cellular T helper type-2 (Th2) phenotype, that is dominated by the pleiotrophic cytokine IL-4. The cellular source of IL-4 has yet to be determined, although basophils have been proposed. Eosinophils and mast cells are
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