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A9972

Sigma-Aldrich

α-Amylase from human pancreas

greener alternative

lyophilized powder, ≥100 units/mg protein

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About This Item

CAS Number:
9000-90-2
Enzyme Commission number:
3.2.1.1 (BRENDA, IUBMB)
EC Number:
232-565-6
MDL number:
MFCD00081319
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

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.

sustainability

Greener Alternative Product

UniProt accession no.

P04746
P19961

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

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P342 + P311

Hazard Classifications

Resp. Sens. 1

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
SLCD4396
SLBZ5414
SLBX5557
SLBX8063
SLBW3203

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Evaluation of an automated system for amylase detection in forensic samples
Vela GD, et al.
International Congress Series, 1288, 636-638 (2006)
Yong Qin Koh et al.
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
Lawrence Quarino et al.
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
G D Brayer et al.
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
Slavica Djonović et al.
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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Protocols

Enzymatic Assay of α-Amylase (EC 3.2.1.1)

Follow our procedure for the determination of alpha-Amylase activity. This enzymatic assay of a-Amylase guides you through the entire process and necessary calculations.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

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