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C7555

Sigma-Aldrich

Concanavalin A from Canavalia ensiformis (Jack bean)

agarose conjugate, Type VI, saline suspension

Synonym(s):

ConA

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About This Item

UNSPSC Code:
12161501
NACRES:
NA.32

biological source

Canavalia ensiformis

Quality Level

conjugate

agarose conjugate

type

Type VI

form

saline suspension

extent of labeling

15-30 mg concanavalin A protein per mL

matrix

cross-linked 4% beaded agarose

matrix activation

cyanogen bromide

matrix attachment

amino

matrix spacer

1 atom

capacity

5-15 mg/mL binding capacity (yeast mannan)

storage temp.

2-8°C

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General description

Concanavalin A (Con A), isolated from Jack beans (Canavalia ensiformis), is a mannose or glucose specific-binding lectin. The lectin is a tetramer and each subunit possesses a saccharide-binding site. Con A can be isolated by affinity chromatography with dextrans.

Application

Concanavalin A (Con A) has been used for enzyme immobilization.
Used for the purification of glycoproteins containing mannose

Biochem/physiol Actions

Concanavalin A (Con A) is a T cell mitogen that can activate the lymphocytes.
Con A can induce tumor cell death through autophagy.
Con A is not blood group specific but has an affinity for terminal α-D-mannosyl and α-D-glucosyl residues. Ca2+ and Mn2+ ions are required for activity. Con A dissociates into dimers at pH 5.6 or below. Between pH 5.8 and pH 7.0, Con A exists as a tetramer; above pH 7.0 higher aggregates are formed. Con A exhibits mitogenic activity which is dependent on its degree of aggregation. Succinylation results in an active dimeric form which remains a dimer above pH 5.6.

Physical form

Suspension in 1.0 M NaCl + 0.1 M potassium phosphate, pH 6.0, with 1 mM CaCl2, 1 mM MgCl2 and 1 mM MnCl2 containing preservative

Analysis Note

Where reported, agglutination activity is expressed in μg/ml and is determined from serial dilutions in phosphate buffered saline, pH 6.8, containing Ca2+ and Mn2+ of a 1 mg per mL solution. This activity is the lowest concentration to agglutinate a 2% suspension of human erythrocytes after 1 hr incubation at 25 °C.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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R Lotan et al.
Biochemistry, 16(9), 1787-1794 (1977-05-03)
The effects of several commonly used detergents on the saccharide-binding activities of lectins were investigated using lectin-mediated agglutination of formalin-fixed erythrocytes and affinity chromatography of glycoproteins on columns of lectins immobilized on polyacrylic hydrazide-Sepharose. In the hemagglutination assays, Ricinus communis
A Kobata et al.
Journal of chromatography, 597(1-2), 111-122 (1992-04-24)
Elucidation of the binding specificity of a concanavalin A-Sepharose column led to the possibility of the affinity chromatography of oligosaccharides and glycopeptides with the use of immobilized lectin columns. Subsequent addition of immobilized erythroagglutinating phytohaemagglutinin, Aleuria aurantia lectin, Datura stramonium
Biosensoric detection of the cysteine sulphoxide alliin
Keusgen M, et al.
Sens. Actuators, 95, 297-302 (2003)
Mai Ly Tran et al.
Traffic (Copenhagen, Denmark), 24(1), 4-19 (2022-11-19)
The trans-Golgi Network (TGN) sorts molecular "addresses" and sends newly synthesized proteins to their destination via vesicular transport carriers. Despite the functional significance of packaging processes at the TGN, the sorting of soluble proteins remains poorly understood. Recent research has
Valentina Carlini et al.
The EMBO journal, 41(7), e108677-e108677 (2022-02-25)
Environmental factors can trigger cellular responses that propagate across mitosis or even generations. Perturbations to the epigenome could underpin such acquired changes, however, the extent and contexts in which modified chromatin states confer heritable memory in mammals is unclear. Here

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