α-amylase is primarily produced in abundance in the salivary glands and pancreas. The expression is also seen in jejunum and mammary glands. The genes encoding α-amylase are AMY1 and AMY2 located in the short arm of chromosome 1. AMY1 is responsible for producing the enzyme in saliva and mammary gland and AMY2 produces the enzyme synthesized in the pancreas. The expression of AMY1 occurs also in certain tumour tissues. Mammalian amylases are composed of three structural domains (A, B and C). Domain A contains the active site with two aspartate and one glutamate residue. Domain B borders the active site region and is essential for maintaining the protein conformation. Domain C is involved in catalytic mechanism.

The antiserum is specific for human a-amylase found in human saliva and human pancreatic extract. No reaction with other human saliva proteins or pancreatic extract proteins is observed.

human salivary α-amylase.

Anti-α-Amylase antibody produced in rabbit has also been used in immunocytochemistry analysis.

Anti-a-Amylase antibody produced in rabbit has been used in immunofluorescence and immunohistochemical analysis.

Mouse pancreatic sections were fixed in 4% paraformaldehyde and used for immunohistochemistry using rabbit anti-amylase antibody at a dilution of 1:100.

α-Amylase is essential for catalyzing the primary step in starch digestion, a main source of carbohydrate in the human diet. α-amylase hydrolysis the polysaccharide with the ultimate production of maltose, maltotriose and limit dextrins as the main products.

Lyophilized from 0.01 M phosphate buffered saline, pH 7.2

Reconstitute with 2 mL deionized water.