L7886
Lectin from Ricinus communis (castor bean) Agglutinin RCA120
buffered aqueous solution
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form
buffered aqueous solution
potency
<4 μg/mL agglutination activity
storage temp.
2-8°C
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General description
Application
Biochem/physiol Actions
Ricinus communis agglutinin (RCA) occurs in two forms designated RCA60 and RCA120 according to their mol. wt. of approx. 60,000 and 120,000 respectively. Neither RCA60 nor RCA120 is blood group specific. RCA60, also referred to as RCAII, Ricin D or RCL III is extremely toxic, inhibits protein synthesis and has an affinity for N-acetyl-D-galactosamine. RCA120, also referred to as RCAI or RCL (I + II), is an agglutinin and has an affinity for terminal β-D-galactosyl residues.
Conjugates are prepared from affinity purified agglutinin RCA120.
Conjugates are prepared from affinity purified agglutinin RCA120.
Physical form
Solution in 0.005 M sodium phosphate and 0.2 M sodium chloride, pH 7.2, containing 0.1% sodium azide
Preparation Note
Purified by affinity chromatography using the method of Lin and Li.[5]
Analysis Note
Agglutination activity is expressed in μg/ml and is determined from serial dilutions in phosphate buffered saline, pH 7.2, of a 1 mg/ml solution. This activity is the lowest concentration to agglutinate a 2% suspension of human erythrocytes after 1 hour incubation at 25 °C.
Storage Class Code
10 - Combustible liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Specificities of Ricinus communis agglutinin 120 interaction with sulfated galactose
Wang Y, et al.
Febs Letters, 585(24), 3927-3934 (2011)
The Lectins: Properties, Functions, and Applications in Biology and Medicine (2012)
A photo-cleavable biotin affinity tag for the facile release of a photo-crosslinked carbohydrate-binding protein
Chang TC, et al.
Bioorganic & Medicinal Chemistry, 24(6), 1216-1224 (2016)
Identification of N-glycosites in chicken egg white proteins using an omics strategy
Geng F, et al.
Journal of Agricultural and Food Chemistry, 65(26), 5357-5364 (2017)
T T Lin et al.
European journal of biochemistry, 105(3), 453-459 (1980-04-01)
Two toxin ricins and two agglutinins have been purified from the seeds of Ricinus communis by an improved procedure based on ion-exchange chromatography and gel filtration. One of the two purified ricins binds to Sepharose 4B while the other does
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