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Ricinus communis agglutinin I is a glycoprotein with a molecular weight of 120,000. The native lectin is moderately toxic and consists of two subunits of 60,000 daltons which can be dissociated by reducing agents into closely related chains between 27,000 and 33,000 daltons. One of the chains appears to be common to the “B” chain of another castor bean lectin, ricin, while the other chain is unique to RCA120. The lectin binds preferentially to oligosaccharides ending in galactose but may also interact with N-acetylgalactosamine. Many glycoproteins have been purified using this lectin since galactose is a common constituent of their oligosaccharide chains. Often, desialylation of the glycoprotein is required first because most glycoproteins have terminal sialic acid residues which can block lectin binding.
Fluorescein labeled Ricinus Communis Agglutinin I is produced by using the highest quality fluorescein isothiocyanate, our affinity-purified lectin, and special conjugation procedures. Fluorescein labeled Ricinus Communis Agglutinin I 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 Ricinus Communis Agglutinin I has an excitation at 495 nm and an emission at about 515 nm. |