ConA Lectin (Biotin) Reference: GTX01504 Concanavalin A is a lectin protein (MW 14kDa), homotetramer 26 kDa; originally extracted from the jack-bean, Canavalia ensiformis. It binds specifically to certain structures found in various sugars α-mannosyl and α-glucosyl residues in glycoproteins. It was the first lectin to be available on a commercial basis and is widely used in biology and biochemistry to characterize glycoproteins and other sugar-containing entities. It is also used to purify macromolecules in lectin affinity chromatography. Concanavalin A interacts with diverse receptors containing mannose carbohydrates (serum and membrane glycoproteins).ConA agglutinate strongly erythrocytes without being blood group specific. Normal cell re agglutinated after trypsinisation. ConA is a also a lymphocyte mitogen.ConA reacts with many bacteria, like E. coli Dictyostelium discoideum et B. substilis It is also widely believed to be involved in the interaction between alpha-mannosyl oligosaccharides on the surface of the HIV virus and the human T cell lymphocyte. Inhibiting/Eluting sugars: 2 α-mM α-methyl mannoside / 2 mM α-methyl glucoside mixture.Carbohydrate-Binding Specificity of Con A: (Manα1,2Manα1,2Man > Manα1,2Man > α-Man > α-Glc > αGlcNAc
ConA Lectin (FITC) Reference: GTX01505 Concanavalin A is a lectin protein (MW 14kDa), homotetramer 26 kDa; originally extracted from the jack-bean, Canavalia ensiformis. It binds specifically to certain structures found in various sugars α-mannosyl and α-glucosyl residues in glycoproteins. It was the first lectin to be available on a commercial basis and is widely used in biology and biochemistry to characterize glycoproteins and other sugar-containing entities. It is also used to purify macromolecules in lectin affinity chromatography. Concanavalin A interacts with diverse receptors containing mannose carbohydrates (serum and membrane glycoproteins).ConA agglutinate strongly erythrocytes without being blood group specific. Normal cell re agglutinated after trypsinisation. ConA is a also a lymphocyte mitogen.ConA reacts with many bacteria, like E. coli Dictyostelium discoideum et B. substilis It is also widely believed to be involved in the interaction between alpha-mannosyl oligosaccharides on the surface of the HIV virus and the human T cell lymphocyte. Inhibiting/Eluting sugars: 2 α-mM α-methyl mannoside / 2 mM α-methyl glucoside mixture.Carbohydrate-Binding Specificity of Con A: (Manα1,2Manα1,2Man > Manα1,2Man > α-Man > α-Glc > αGlcNAc
Peanut Lectin Reference: GTX01506 Peanut lectin (PNA) is an identical tetrameric carbohydrate free protein with MW of 11 kDa. Thomsen-Friedenreich antigen, T-antigen (Galβ1, 3GalNAc) is present on blood group M &N glycoproteins (after removal of sialic acid with neuraminidase), glyconjugates (Mucin type), gangliosides and many glycolipids. T antigen is rarely expressed on normal coloncytes whereas cells of malignant, premalignant cells express this antigen. Peanut lectin has widely been used to detect T antigen in malignant and premalignant cells. Peanut lectin contains one atom of Ca++ and Mg++ per unit. Inhibiting/Eluting sugars: 2 mM GalactoseCarbohydrate-Binding Specificity of PNA: Galβ1, 3 GalNAc>>>>>GalNAc>Gal
Peanut Lectin (Biotin) Reference: GTX01507 Peanut lectin (PNA) is an identical tetrameric carbohydrate free protein with MW of 11 kDa. Thomsen-Friedenreich antigen, T-antigen (Galβ1, 3GalNAc) is present on blood group M &N glycoproteins (after removal of sialic acid with neuraminidase), glyconjugates (Mucin type), gangliosides and many glycolipids. T antigen is rarely expressed on normal coloncytes whereas cells of malignant, premalignant cells express this antigen. Peanut lectin has widely been used to detect T antigen in malignant and premalignant cells. Peanut lectin contains one atom of Ca++ and Mg++ per unit. Inhibiting/Eluting sugars: 2 mM GalactoseCarbohydrate-Binding Specificity of PNA: Galβ1, 3 GalNAc>>>>>GalNAc>Gal
Peanut Lectin (FITC) Reference: GTX01508 Peanut lectin (PNA) is an identical tetrameric carbohydrate free protein with MW of 11 kDa. Thomsen-Friedenreich antigen, T-antigen (Galβ1, 3GalNAc) is present on blood group M &N glycoproteins (after removal of sialic acid with neuraminidase), glyconjugates (Mucin type), gangliosides and many glycolipids. T antigen is rarely expressed on normal coloncytes whereas cells of malignant, premalignant cells express this antigen. Peanut lectin has widely been used to detect T antigen in malignant and premalignant cells. Peanut lectin contains one atom of Ca++ and Mg++ per unit. Inhibiting/Eluting sugars: 2 mM GalactoseCarbohydrate-Binding Specificity of PNA: Galβ1, 3 GalNAc>>>>>GalNAc>Gal
Peanut Lectin (PE) Reference: GTX01509 Peanut lectin (PNA) is an identical tetrameric carbohydrate free protein with MW of 11 kDa. Thomsen-Friedenreich antigen, T-antigen (Galβ1, 3GalNAc) is present on blood group M &N glycoproteins (after removal of sialic acid with neuraminidase), glyconjugates (Mucin type), gangliosides and many glycolipids. T antigen is rarely expressed on normal coloncytes whereas cells of malignant, premalignant cells express this antigen. Peanut lectin has widely been used to detect T antigen in malignant and premalignant cells. Peanut lectin contains one atom of Ca++ and Mg++ per unit. Inhibiting/Eluting sugars: 2 mM GalactoseCarbohydrate-Binding Specificity of PNA: Galβ1, 3 GalNAc>>>>>GalNAc>Gal
UEA I Lectin Reference: GTX01510 The anti-H (O) hemagglutinating activity of Ulex europaeus has been used widely to confirm blood group O activity. UEA I binds to many glycoproteins and glycolipids containing α –linked fucose residue. The purified lectin appears to be a dimer of two distinct polypeptide chains associated by noncovalent forces. This lectin does not react with Lea active blood group substance. The native protein has pI=6.-6.1 and exhibits a Molecular weight 6,-68, during gel filtration on Sephadex column. This lectin will hemagglutinate fresh blood group O cells at 2-5μg/ml.Inhibiting/Eluting sugars: 5-1 mM L-fucoseCarbohydrate-Binding Specificity of UEA I: L-Fuα1,2Galβ1,4GlcNAcβ1,6R
UEA I Lectin (Biotin) Reference: GTX01511 The anti-H (O) hemagglutinating activity of Ulex europaeus has been used widely to confirm blood group O activity. UEA I binds to many glycoproteins and glycolipids containing α –linked fucose residue. The purified lectin appears to be a dimer of two distinct polypeptide chains associated by noncovalent forces. This lectin does not react with Lea active blood group substance. The native protein has pI=6.-6.1 and exhibits a Molecular weight 6,-68, during gel filtration on Sephadex column. This lectin will hemagglutinate fresh blood group O cells at 2-5μg/ml.Inhibiting/Eluting sugars: 5-1 mM L-fucoseCarbohydrate-Binding Specificity of UEA I: L-Fuα1,2Galβ1,4GlcNAcβ1,6R
UEA I Lectin (FITC) Reference: GTX01512 The anti-H (O) hemagglutinating activity of Ulex europaeus has been used widely to confirm blood group O activity. UEA I binds to many glycoproteins and glycolipids containing α –linked fucose residue. The purified lectin appears to be a dimer of two distinct polypeptide chains associated by noncovalent forces. This lectin does not react with Lea active blood group substance. The native protein has pI=6.-6.1 and exhibits a Molecular weight 6,-68, during gel filtration on Sephadex column. This lectin will hemagglutinate fresh blood group O cells at 2-5μg/ml.Inhibiting/Eluting sugars: 5-1 mM L-fucoseCarbohydrate-Binding Specificity of UEA I: L-Fuα1,2Galβ1,4GlcNAcβ1,6R