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L7886

Sigma-Aldrich

Lectin from Ricinus communis (castor bean) Agglutinin RCA120

buffered aqueous solution

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About This Item

Numéro MDL:
MFCD00165777
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

Forme

buffered aqueous solution

Puissance

<4 μg/mL agglutination activity

Température de stockage

2-8°C

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Description générale

Lectins are carbohydrate binding proteins. Lectin from Ricinus communis (castor bean) Agglutinin RCA120 is purified from the seeds of the castor plant. It is a tetrameric hemagglutinin with two α and two β subunits.

Application

Lectin from Ricinus communis (castor bean) Agglutinin RCA120 has been used for the digestion, enrichment and deglycosylation of chicken egg white (CEW) glycopeptides. It has also been used as a model carbohydrate-binding protein.

Actions biochimiques/physiologiques

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.
Lectin from Ricinus communis (castor bean) Agglutinin RCA120 is used to study cell surface glycoproteins the separation of glycoproteins with Galβ-terminating oligosaccharide chains from glycolipids. Lectin agglutinates cells and precipitates polysaccharides and glycoproteins.

Forme physique

Solution in 0.005 M sodium phosphate and 0.2 M sodium chloride, pH 7.2, containing 0.1% sodium azide

Notes préparatoires

Purified by affinity chromatography using the method of Lin and Li.

Remarque sur l'analyse

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.

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

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Certificats d'analyse (COA)

Lot/Batch Number
11131027
074M4118V
0000094672
019M4091V
11141024

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Consulter la Bibliothèque de documents

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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