Amylases are secreted proteins that hydrolyze 1,4 alpha glucoside bonds in oligosaccharides and polysaccharides. They catalyze the first step in digestion of dietary starch and glycogen. Alternative splicing results in multiple transcript variants encoding the same protein.||Contaminants: Lipase: <0.001%; Proteases: <0.001%; Ammonia: <0.001Umole/mg||Source: |Amylase alpha, from human saliva.||Activity:|~120 Units/mg powder @ 37°C|\t|Protein:|~0.4mg Protein/mg powder (Coomassie)|\t|Specific Activity:|~300 Units/mg Protein|\t|Unit Definition:|One unit will catalyze the hydrolysis of one micromole of malto pentaose, which through coupled reactions results in the formation of 5 micromoles of glucose-6-phosphate per minute at 37°C. Measured at 340nm as an equimolar amount of NADH produced by a coupled reaction.||Storage and Stability:|Lyophilized powder may be stored at -20°C. Reconstitute with sterile buffer or ddH2O. Aliquot and store at -20°C. Reconstituted product is stable for 6 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.Source: Human Saliva|Purity: ~90% (SDS-PAGE).|Concentration: Not determined |Form: Supplied as a lyophilized powder from 20mM Tris, pH 7.2, 150mM sodium chloride, 1mM calcium chloride. Reconstitute with Tris saline or other buffer.||Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.

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