Proteins and Derivatives
Proteins and Derivatives
Vector Laboratories Vicia Villosa Lectin (VVL, VVA) Biotinylated 2 mg
Vicia villosa lectin (VVL, VVA) preferentially binds α- or β-linked terminal N-acetylgalactosamine, especially a single α-N-acetylgalactosamine residue linked to serine or threonine in a polypeptide (the Tn antigen). This lectin may require specific amino acid sequences at the receptor site of glycosylation, and the disaccharide galactosyl (α-1,3) N-acetylgalactosamine is also a potent inhibitor. 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.
Vector Laboratories Vicia Villosa Lectin (VVL, VVA), Fluorescein 2mg
VVL recognizes preferentially α- or β-linked terminal N-acetylgalactosamine, especially a single α-N-acetylgalactosamine residue linked to serine or threonine in a polypeptide (the Tn antigen). Evidence suggests that this lectin also may require specific amino acid sequences at the receptor site of glycosylation. The disaccharide galactosyl (α-1,3) N-acetylgalactosamine is also a potent inhibitor of this lectin.Fluorescein labeled Vicia villosa lectin has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated fluorochromes. The excitation maximum is at 495 nm and the emission maximum is at 515 nm.
Vector Laboratories Vicia Villosa Lectin (VVL VVA) Agarose Bound 2 ml
Vicia villosa lectin (VVL) includes a family of tetrameric glycoproteins consisting of combinations of A and B subunits, though the dominant isolectins in our preparations appear to be B subunit-rich. VVL recognizes α- or β-linked terminal N-acetylgalactosamine, especially a single α-N-acetylgalactosamine residue linked to serine or threonine in a polypeptide (the Tn antigen). Binding may also require specific amino acid sequences at the receptor site of glycosylation. This agarose-bound VVL is prepared using affinity-purified lectin and heat stable, cross-linked 4% agarose beads. The attachment of the lectin through a hydrophilic spacer arm to the beads is carefully controlled to preserve the activity and minimize conformational changes to the bound lectins. The recommended inhibiting/eluting sugar is 200 mM N-acetylgalactosamine.