L5390
Lectin from Erythrina cristagalli (coral tree)
lyophilized powder
Synonym(s):
Erythrina cristagalli agglutinin, ECA
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About This Item
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form
lyophilized powder
Quality Level
potency
<0.5 μg per mL agglutination activity
composition
Protein, ≥85% biuret
impurities
salt, free
storage temp.
−20°C
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Biochem/physiol Actions
Lectin or haemagglutinin is a sugar stereospecific binding protein or glycoprotein. It is capable of reversibly agglutinating cells. It is implicated in various cellular processes such as cell agglutination, homing of leukocytes, induction of mitosis in lymphocytes, interferon c (IFN c) and cytotoxicity. It is used as a blood typing reagent in immunohaematology. Lectin is also used as a reagent in testing erythrocyte polyagglutinable states. It is considered as a potential tool for analyzing cell surface architecture and related membrane functions.
ECA is not blood group specific, but has an affinity for D-galactose and D-galactosides. It is reported to be mitogenic for human peripheral blood T lymphocytes.
Preparation Note
Purified by affinity chromatography.
Analysis Note
Agglutination activity is expressed in μg/ml and is determined from serial dilutions in phosphate buffered saline, pH 6.8, of a 1 mg per mL solution. This activity is the lowest concentration to agglutinate a 2% suspension of trypsinized human blood group O erythrocytes after 1 hr at 25 °C.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Human erythrocyte specific lectin from the seeds of Indian coral tree, Erythrina variegata Linn, var. orientali Linn, Merrill
Datta TK and Basu PS
Journal of Biosciences, 5(1), 25-30 (1983)
Purification, some properties of a D-galactose-binding leaf lectin from Erythrina indica and further characterization of seed lectin
Konozy EHE, et al.
Biochimie, 84(10), 1035-1043 (2002)
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