C7555
Concanavalin A from Canavalia ensiformis (Jack bean)
agarose conjugate, Type VI, saline suspension
Synonym(s):
ConA
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
UNSPSC Code:
12161501
NACRES:
NA.32
Recommended Products
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
storage temp.
2-8°C
Looking for similar products? Visit Product Comparison Guide
Related Categories
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 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.
Signal Word
Danger
Hazard Statements
Precautionary 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)
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
Biosensoric detection of the cysteine sulphoxide alliin
Keusgen M, et al.
Sens. Actuators, 95, 297-302 (2003)
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
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
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
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service