Allium sativum Lectin (ASA) - Biotinylated

Allium sativum lectin (ASA) is isolated from garlic bulbs and purified with affinity chromatography. It is a dimer of two subunits. ASA binds to several α1-2-linked mannose residues. The lectin recognizes internal mannose and binds to the core pentasaccharide of N-linked glycans. In addition, the removal of sialic acids enhances binding activity. The binding site can withstand terminal sialic acid and galactose residues. The blood group specificity of ASA is towards rabbit erythrocytes and weak interaction with human erythrocytes. ASA has shown antiproliferative and apoptosis-inducing activity, making it a relative subject in cancer research.

Biotin is a small molecule involved in a wide range of metabolic processes. This ligand forms a complex with Avidin and Streptavidin, resulting in the strongest non-covalent protein-ligand interaction known. Biotinylated Allium sativum Lectin (ASA) has an appropriate amount of biotin bound to provide optimum detection characteristics when using an Avidin-HRP or Streptavidin-HRP conjugate. Biotinylated lectins allow for more sensitive detection in ELISA and Western-blotting applications.

Applications: Immunocytochemistry, Immunofluorescence, Western blotting, Immunohistochemistry, Glycobiology.

Recommended Usage: Recommended dilution ranges 0.5 – 10 µg/ml. 1XPBS can be used for reconstitution. Less than 0.5 ug /ml will agglutinate rabbit erythrocytes.

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Storage Instruction: To prevent degradation and avoid repeated freeze-thaw cycles, aliquot your product into small, single-use volumes and store them at -20°C