A9972
α-Amylase from human pancreas
lyophilized powder, ≥100 units/mg protein
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About This Item
biological source
human pancreas
form
lyophilized powder
specific activity
≥100 units/mg protein
purified by
2× crystallization
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
greener alternative category
, Enabling
storage temp.
−20°C
Gene Information
human ... AMY1A(279) , AMY2B(280)
General description
We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in starch ethanol research. For more information see the article in biofiles.
Biochem/physiol Actions
α-Amylase is composed of 496 amino acids in a single polypeptide chain. It hydrolyzes the α-(1,4) glucan linkages in polysaccharides of three or more α-(1,4) linked D-glucose units. Natural substrates such as starch and glycogen are broken down into glucose and maltose.
Unit Definition
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.
Physical form
Lyophilized from Tris buffer containing NaCl and CaCl2.
Preparation Note
Prepared by modified method of Levitzki et al.
Other Notes
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
Certificates of Analysis (COA)
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Evaluation of an automated system for amylase detection in forensic samples
International Congress Series, 1288, 636-638 (2006)
Heliyon, 8(8), e10131-e10131 (2022-08-23)
Carbohydrate digestibility is a key determinant for elevated postprandial hyperglycemia (PPHG). Apart from dietary restrictions, one of the strategies to reduce PPHG is to limit the activity of carbohydrate digestive enzymes within the gastrointestinal tract in order to reduce monosaccharide
Journal of forensic sciences, 50(4), 873-876 (2005-08-05)
An ELISA method for the detection of salivary amylase in dried stains using a monoclonal anti-human salivary amylase antibody was developed. Studies demonstrated the assay to be sensitive down to 0.0002 Sigma units and showed a linear response between absorbance
Protein science : a publication of the Protein Society, 4(9), 1730-1742 (1995-09-01)
The structure of human pancreatic alpha-amylase has been determined to 1.8 A resolution using X-ray diffraction techniques. This enzyme is found to be composed of three structural domains. The largest is Domain A (residues 1-99, 169-404), which forms a central
PLoS pathogens, 9(3), e1003217-e1003217 (2013-03-19)
Pseudomonas aeruginosa strain PA14 is a multi-host pathogen that infects plants, nematodes, insects, and vertebrates. Many PA14 factors are required for virulence in more than one of these hosts. Noting that plants have a fundamentally different cellular architecture from animals
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