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Key Documents

A9972

Sigma-Aldrich

α-Amylase from human pancreas

greener alternative

lyophilized powder, ≥100 units/mg protein

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About This Item

Numero CAS:
Classificazione EC (Enzyme Commission):
Numero CE:
Numero MDL:
Codice UNSPSC:
12352204
eCl@ss:
32160410
NACRES:
NA.54

Origine biologica

human pancreas

Forma fisica

lyophilized powder

Attività specifica

≥100 units/mg protein

Purificato mediante

2× crystallization

Caratteristiche più verdi

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

sustainability

Greener Alternative Product

N° accesso UniProt

Categoria alternativa più verde

Temperatura di conservazione

−20°C

Informazioni sul gene

Descrizione generale

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.

Azioni biochim/fisiol

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.

Definizione di unità

One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.

Stato fisico

Lyophilized from Tris buffer containing NaCl and CaCl2.

Nota sulla preparazione

Prepared by modified method of Levitzki et al.

Pittogrammi

Health hazard

Avvertenze

Danger

Indicazioni di pericolo

Consigli di prudenza

Classi di pericolo

Resp. Sens. 1

Codice della classe di stoccaggio

13 - Non Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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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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