Vicia villosa Lectin (VVL/VVA) - Pure
Vicia villosa lectin or agglutinin (VVL/VVA) is isolated from hairy vetch seeds and purified by affinity chromatography. It is a tetramer composed of four subunits and a molecular weight of 144,000. It has an isoelectric point between pH 5.5 and pH 6.2. VVL consists of A and B subunits, with a dominant isolectin that appears to be B subunit-rich. A4 isolectin agglutinates specifically A1 erythrocytes, B4 isolectin agglutinates Tn exposed erythrocytes but does not agglutinate A, B, or O-erythrocytes, and A2B2 isolections display properties characteristic of both A4 and B4 isolections.
VVLB4 binds specifically to GalNAc structures, and studies suggest that this lectin binds only to the terminal GalNAc structure, rather than both the internal and terminal structures. VVL interacts with the terminal ?-linked Gal over GalNAc, and displays a weaker binding to ?-linked GalNAc and Gal compared to ?-linked counterparts.
This product comes in a lyophilized form and is stored at -20ºC. Reconstitute with sterile buffer. Metal ions calcium and manganese are required for binding.
|Molecular Weight||:||144 kDa|
|Shelf Life||:||2 years|