Mini Gastrin I, human Reference: HY-P1593 Mini Gastrin I, human is a shorter version of human gastrin, consists of amino acids 5-17 of the parent peptide.
WGA Lectin (FITC) Reference: GTX01502 Wheat germ agglutinin (WGA) (MW 36 kDa) is a dimeric, carbohydrate-free protein composed of two identical subunits. The amino acid sequence provides a figure of 21,6, based on 171 amino acids per polypeptide chain. The protein dissociates into monomers in acidic media, pK of the reaction 4. The receptor sugar for WGA is N-acetyl glucosamine (GlcNAc), GlcNacβ14GlcNAc. These structures are present in many serum and membrane glycoproteins, bacterial cell wall peptidoglycans, chitin, cartilage glycosaminogyycons and glycolipids. Native WGA also react with glycoproteins with sialic acid residue. This lectin is useful for the purification of insulin receptors, serum proteins and neuronal tracing. The carbohydrate-binding specificity of WGA has been studied by variety of techniques, such as hapten inhibition of hemagglutination and specific precipitation of glycoconjugate, changes in fluorescence of the lectin (intrinsic) or of chromatogenic ligands (extrinsic), equilibrium dialysis, NMR and x-ray diffraction. Inhibiting/Eluting sugars: 5 mM GlcNAc, dimer, trimmer or 1 mM acetic acid.Carbohydrate-Binding Specificity of WGA: Pentaacetylchitopentaose >Tetraacetylchitotetraose > triacetylchitotriose > Diacetylchitobiose > GlcNAc
ConA Lectin Reference: GTX01503 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
L-Phenylalanylglycylglycine Reference: HY-W009345 L-Phenylalanylglycylglycine is a Glycine (HY-Y0966) derivative.
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
Barusiban Reference: HY-P3516 Barusiban (FE-200440) is an oxytocin receptor (OT-R) antagonist (Ki=0.8 nM), inhibits OT-induced contraction. Barusiban can be used in preterm labor (PTL), in vitro fertilisation (IVF) and infertility research.
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
Enhanced Green Fluorescent Protein (EGFP) (200-208) Reference: HY-P2528 Enhanced Green Fluorescent Protein (EGFP) (200-208) is a marker gene product derived from the jellyfish Aequorea Victoria. Enhanced Green Fluorescent Protein (EGFP) (200-208) is a common reporter protein and is easy to detect.
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