11028-71-0
Showing all 8 results
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Concanavalin A
$66.57 Add to cart View Product DetailsConcanavalin A
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Concanavalin A
$137.45 Add to cart View Product DetailsConcanavalin A
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Concanavalin A
$223.01 Add to cart View Product DetailsConcanavalin A
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Concanavalin A
$295.83 Add to cart View Product DetailsConcanavalin A
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Concanavalin A, highly purified
$138.48 Add to cart View Product DetailsPure Canavalia ensiformis lectin (Con A) from Jackbean. Isolated by affinity chromatography on cross-linked dextran. Con A exists as a dimer below pH 5.0 and and at pH >7 it exists as a tetramer. Con-A is not a glycoprotein. The monomeric molecular weight of Con-A is 25,500. Con-A does not contain cysteine residues. Unlike most other lectins, Con-A is a metalloprotein and requires a transition metal ion, such as manganese, plus calcium ions for binding. Lectins are proteins or glycoproteins of non-immune origin that agglutinate cells and/or precipitate complex carbohydrates. Lectins are capable of binding glycoproteins even in presence of various detergents. The agglutination activity of these highly specific carbohydrate-binding molecules is usually inhibited by a simple monosaccharide, but for some lectins, di, tri, and even polysaccharides are required.
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Concanavalin A, highly purified
$222.61 Add to cart View Product DetailsPure Canavalia ensiformis lectin (Con A) from Jackbean. Isolated by affinity chromatography on cross-linked dextran. Con A exists as a dimer below pH 5.0 and and at pH >7 it exists as a tetramer. Con-A is not a glycoprotein. The monomeric molecular weight of Con-A is 25,500. Con-A does not contain cysteine residues. Unlike most other lectins, Con-A is a metalloprotein and requires a transition metal ion, such as manganese, plus calcium ions for binding. Lectins are proteins or glycoproteins of non-immune origin that agglutinate cells and/or precipitate complex carbohydrates. Lectins are capable of binding glycoproteins even in presence of various detergents. The agglutination activity of these highly specific carbohydrate-binding molecules is usually inhibited by a simple monosaccharide, but for some lectins, di, tri, and even polysaccharides are required.
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Concanavalin A, highly purified
$45.15 Add to cart View Product DetailsPure Canavalia ensiformis lectin (Con A) from Jackbean. Isolated by affinity chromatography on cross-linked dextran. Con A exists as a dimer below pH 5.0 and and at pH >7 it exists as a tetramer. Con-A is not a glycoprotein. The monomeric molecular weight of Con-A is 25,500. Con-A does not contain cysteine residues. Unlike most other lectins, Con-A is a metalloprotein and requires a transition metal ion, such as manganese, plus calcium ions for binding. Lectins are proteins or glycoproteins of non-immune origin that agglutinate cells and/or precipitate complex carbohydrates. Lectins are capable of binding glycoproteins even in presence of various detergents. The agglutination activity of these highly specific carbohydrate-binding molecules is usually inhibited by a simple monosaccharide, but for some lectins, di, tri, and even polysaccharides are required.
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Concanavalin A, highly purified
$449.51 Add to cart View Product DetailsPure Canavalia ensiformis lectin (Con A) from Jackbean. Isolated by affinity chromatography on cross-linked dextran. Con A exists as a dimer below pH 5.0 and and at pH >7 it exists as a tetramer. Con-A is not a glycoprotein. The monomeric molecular weight of Con-A is 25,500. Con-A does not contain cysteine residues. Unlike most other lectins, Con-A is a metalloprotein and requires a transition metal ion, such as manganese, plus calcium ions for binding. Lectins are proteins or glycoproteins of non-immune origin that agglutinate cells and/or precipitate complex carbohydrates. Lectins are capable of binding glycoproteins even in presence of various detergents. The agglutination activity of these highly specific carbohydrate-binding molecules is usually inhibited by a simple monosaccharide, but for some lectins, di, tri, and even polysaccharides are required.
