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L5390

Sigma-Aldrich

Lectin from Erythrina cristagalli (coral tree)

lyophilized powder

Sinónimos:

Erythrina cristagalli agglutinin, ECA

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About This Item

MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32

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

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificados de análisis (COA)

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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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