Test
The Phytohemagglutinin-L (PHA-L) Solution (500X) is a ready to use solution of PHA-L in aqueous buffer.
Product Type | Phytohemagglutinin-L (PHA-L) Solution |
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Product Line | eBioscience™ |
Phytohemagglutinin, Phaseolus Vulgaris is crude Phaseolus vulgaris-P lectin (PHA-P) from the Red Kidney Bean.
Lens Culinaris Agglutinin (LCA), fluorescein ( FITC), is a bright-green LCA-fluorophore conjugate that is sourced from a common edible lentil.
isolated from wheat germ, dissolved in 0.05 M Tris-HCl, 0.15 M NaCl buffer, pH 8.6 and purified by affinity chromatography
NC2944062 AGGLUTININ 2MG
CF640R RABBIT ANTI-RFP 1MGML 100UL
Wheat germ agglutinin (WGA) binds N-acetylglucosamine, preferentially to dimers and trimers of this sugar. It can bind oligosaccharides containing terminal N-acetylglucosamine or chitobiose, structures common to many serum and membrane glycoproteins. Bacterial cell wall peptidoglycans, chitin, cartilage glycosaminoglycans, and glycolipids can also bind WGA. Native WGA also interacts with some glycoproteins via sialic acid residues (see succinylated WGA). This conjugate features a ratio of biotin to lectin protein that provides optimal avidin/streptavidin and lectin binding activity. Supplied essentially free of unconjugated biotins, it is preserved with sodium azide.
Peanut agglutinin (PNA) binds preferentially to the T-antigen, a galactosyl (β-1,3) N-acetylgalactosamine structure present in many glycoconjugates such as M and N blood groups, gangliosides, and other soluble and membrane-associated glycoproteins and glycolipids. With some exceptions, the PNA receptor sequence is normally sialylated, which prevents the lectin from binding to its receptor oligosaccharide (see Jacalin). Even sialic acid that is not bound directly to the receptor sugars may inhibit binding. The presence of calcium ions in diluents can enhance the binding of PNA to receptors, possibly by neutralizing the negative charges on sialic acid residues adjacent to the receptor sequence. This conjugate features a ratio of biotin to lectin protein that provides optimal avidin/streptavidin and lectin binding activity. Supplied essentially free of unconjugated biotins, it is preserved with sodium azide.
Wheat germ agglutinin (WGA) contains a group of closely related isolectins that bind N-acetylglucosamine (preferentially the dimers and trimers of this sugar) and oligosaccharides containing terminal N-acetylglucosamine or chitobiose, structures common to many serum and membrane glycoproteins. Bacterial cell wall peptidoglycans, chitin, cartilage glycosaminoglycans, and glycolipids can also bind WGA. Native WGA also interacts with some glycoproteins via sialic acid residues (see succinylated WGA). This unconjugated WGA is used for the purification of insulin receptors and for neuronal tracing and is supplied as a solution preserved with sodium azide. The recommended inhibiting/eluting sugar is chitin hydrolysate or 500 mM N-acetylglucosamine with salt and/or acid elution.
Ulex europaeus agglutinin I (UAE I) binds to glycoproteins and glycolipids containing α-linked fucose residues, such as ABO blood group glycoconjugates. This lectin preferentially binds blood group O cells and has been used to determine secretor status. It is also an established marker for human endothelial cells. This rhodamine-labeled UAE I features a ratio of fluorophore to lectin protein that provides optimal staining (excitation 575 nm, emission 600 nm) and is supplied in solution, essentially free of unconjugated fluorophore.
NC2035898 WHEAT GERM AGGLUTININ CF770
Wheat germ agglutinin WGA is a lectin that binds to N-acetyl-D-glucosamine and sialic acid. This catalog is for 1 mg.