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Compound 48/80

Compound E

Compound E

Concanamycin A (High purity)

Concanamycin A (High purity)

Concanavalin A

Concanavalin A

Concanavalin A

Concanavalin A

Concanavalin A

Concanavalin A, Fitc Conjugated

Concanavalin A, Fitc Conjugated

Pure 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.

Pure 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.

Pure 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.

Pure 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.

Wash solution included in the FastDNA and all FastDNA Spin Kits. Used to remove impurities once the DNA is bound to the Binding Matrix