Allium sativum Lectin (ASA) - AP (Alkaline Phosphatase)

Allium sativum lectin (ASA) is isolated from garlic 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 Penta-saccharide of N-linked glycans. In addition, the removal of sialic acids enhances binding activity.  ASA has shown antiproliferative and apoptosis-inducing activity, making it a relative subject in cancer research.

Alkaline phosphatase is a large protein (140 kDa) that catalyzes the hydrolysis of phosphate groups from a substrate resulting in a colored or fluorescent product. The optimal enzymatic activity of this protein is between pH 8 and 10, and its reaction rate remains linear, improving sensitivity over time.

Applications: Immunofluorescence, Immunohistochemistry, Western blot, ELLA/ELISA

Recommended Usage: Recommended dilution range 0.5-10 ug/ml. 1XPBS can be used to dilute the stocks.

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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