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AVANTI POLAR LIPIDS , CYGNUS , LARODAN , ADIPOGEN , MYBIOSOURCE , SERVA NORDMARK, BIOWORLD, EDGEBIO , PANREAC APPLICHEM
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Product Description
Lectin concanavalin A (Con A) is isolated from jack bean seeds (Canavalia ensiformis) and purified by affinity chromatography. Con A is composed of identical subunits of 237 amino acid residues (MW: 26,000 without any cystine residues) and while above pH 7 it is predominantly tetrameric, itâ€s optimal activity is near pH 7 (at pH 4.5 - 5.6, Con A exists as a single dimer MW: 53,000). Con A has a carbohydrate specificity toward α-mannose and α-Glc, eluting a concentration of 0.2M MeαMan + MeαGlc.
Con A binds two metal ions per monomer: a transition metal, nominally Mn2+ and Ca2+. Both ions are required for saccharide binding with optimum activity at a pH 7.0. Con A binds with non-reducing α-D-glucose, α-D-mannose and α-methyl-D-glucopyranoside acts as a competitive inhibitor.
Con A exhibits mitogenic activity with lymphocytes and cancer cells which aggregate by Con A; normal white cells do not. Normal cells react to Con A after proteolytic treatment which suggests that trypsinization causes clustering of the reactive glycan residues on the membrane.
Studies of Con A interaction with particular cell types include locust muscle fibers, adipocytes, and rat liver plasma membrane components. Con A induces endoreduplication in mammalian cells and it reacts with E. coli, Dictyostelium discoideum Bacillus lipopolysaccharide.
Immobilized Con A has been used in affinity chromatography purifications of a wide variety of glycoproteins and cellular structures.
Con A comes in lyophilized powder form and is stable for more than five years from production date when stored below -20 C. Con A has non-specific blood group.
Applications:
Hormone receptor studies
Lymphocyte mitogenic studies
Characterization of certain normal and malignant cells
Affinity chromatography
References
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