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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

Número CAS:
Número da licença da enzima:
Número CE:
Número MDL:
Código UNSPSC:
12352204
eCl@ss:
32160410
NACRES:
NA.54

fonte biológica

human pancreas

forma

lyophilized powder

atividade específica

≥100 units/mg protein

purificado por

2× crystallization

características do produto alternativo mais ecológico

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

sustainability

Greener Alternative Product

nº de adesão UniProt

categoria alternativa mais ecológica

temperatura de armazenamento

−20°C

Informações sobre genes

Descrição geral

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.

Ações bioquímicas/fisiológicas

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.

Definição da unidade

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

forma física

Lyophilized from Tris buffer containing NaCl and CaCl2.

Nota de preparo

Prepared by modified method of Levitzki et al.

Pictogramas

Health hazard

Palavra indicadora

Danger

Frases de perigo

Declarações de precaução

Classificações de perigo

Resp. Sens. 1

Código de classe de armazenamento

13 - Non Combustible Solids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (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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