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Galanthus nivalis lectin is a small molecular weight tetramer consisting of subunits of about 13,000 daltons. It has an isoelectric point below pH 4.6. The lectin contains little or no carbohydrate and, unlike most mannose-specific lectins, is not a metalloprotein and does not require Ca++ or Mn++ for binding.
Binding seems to be preferentially directed toward structures containing (a-1,3) mannose residues. Also in contrast to most mannose-binding lectins, GNL will not bind alpha linked glucose. Reports indicate that this lectin binds IgM but not IgG of the immunoglobulin classes of rat and mouse. The only protein from human serum reported to bind to this lectin is a2-macroglobulin.
Fluorescein labeled Galanthus Nivalis Lectin is produced by using the highest quality fluorescein isothiocyanate, our affinity-purified lectin, and special conjugation procedures. Fluorescein labeled Galanthus Nivalis Lectin has an appropriate number of fluorochromes bound which provide the maximum fluorescence and optimum staining characteristics for this particular lectin. This lectin is supplied essentially free of unconjugated fluorochromes and inactive lectin. Fluorescein labeled Galanthus Nivalis Lectin has an excitation at 495 nm and an emission at about 515 nm. |