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Merck

A4268

α-Amylase aus Schweinepankreas

greener alternative

Type I-A, PMSF treated, saline suspension, 700-1400 units/mg protein (E1%/280)

Synonym(e):

β-N-Acetylglucosaminidase, Schweineplazenta, PPA, Schweinepankreas α-Amylase, al1,4-Glucan-4-glucanohydrolase,

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25 MG

€ 337,00

€ 337,00


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Über diesen Artikel

UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54
MDL number:
Specific activity:
700-1400 units/mg protein (E1%/280)
Biological source:
Porcine pancreas

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biological source

Porcine pancreas

type

Type I-A

form

saline suspension

specific activity

700-1400 units/mg protein (E1%/280)

mol wt

51-54 kDa

greener alternative product characteristics

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

sustainability

Greener Alternative Product

technique(s)

activity assay: suitable

suitability

suitable for hydrolysis, synthesis of oligosaccharides and polysaccharides, and sugar modification

application(s)

diagnostic assay manufacturing

greener alternative category

storage temp.

2-8°C

Quality Level

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Dieser Artikel
A6255A3403A3176
biological source

Porcine pancreas

biological source

Porcine pancreas

biological source

-

biological source

Porcine pancreas

specific activity

700-1400 units/mg protein (E1%/280)

specific activity

≥1000 units/mg protein (E1%/280)

specific activity

≥500 units/mg protein (biuret)

specific activity

≥5 units/mg solid

technique(s)

activity assay: suitable

technique(s)

-

technique(s)

-

technique(s)

activity assay: suitable

application(s)

diagnostic assay manufacturing

application(s)

-

application(s)

-

application(s)

life science and biopharma

form

saline suspension

form

saline suspension

form

saline solution

form

powder

suitability

suitable for hydrolysis, synthesis of oligosaccharides and polysaccharides, and sugar modification

suitability

-

suitability

-

suitability

suitable for hydrolysis, synthesis of oligosaccharides and polysaccharides, and sugar modification

General description

Molekülmasse: 51–54 kDa.
α-Amylase, isoliert aus Schweine-Pankreas, ist ein Glykoprotein. Sie ist eine einzelne Polypeptidkette von ~475 Resten, die zwei SH-Gruppen und vier Disulfidbrücken sowie dicht gebundenes Ca2+ für die Stabilität enthält. Chloridionen sind notwendig für Aktivität und Stabilität. Der pH-Wertbereich für Aktivität beträgt 5,5 bis 8,0, wobei der optimale pH-Wert bei 7 liegt.
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.

Application

α-Amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. α-Amylase, from Sigma, has been used in various plant studies, such as metabolism studies in Arabidopsis [1].

Biochem/physiol Actions

α-Amylase 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. α -Amylase, from porcine pancreas, is a glycoprotein that consists of a single polypeptide chain of approximately 475 residues containing 2 SH groups and four disulfide bridges and a tightly bound Ca2+ necessary for stability.

Physical form

Suspension in 2.9 M NaCl-Lösung, enthält 3 mM CaCl2.

Preparation Note

2x kristallisiert

Other Notes

1 U setzt 1.0 mg Maltose aus Stärke in 3 Minuten frei bei pH 6.9 und 20 °C.

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pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Lagerklasse

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves


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Doudou Huang et al.
Drug design, development and therapy, 15, 5001-5010 (2021-12-25)
Diabetes is a common disease caused by a combination of genetic and environmental factors, which was the top three diseases threatening human health. Therefore, it is necessary to seek more efficient hypoglycemic drugs. The main objective of this study was
Lijiao Kan et al.
Food chemistry, 361, 130047-130047 (2021-05-25)
Inhibition of maltase, sucrase, isomaltase and glucoamylase activity by acarbose, epigallocatechin gallate, epicatechin gallate and four polyphenol-rich tea extract from white, green, oolong, black tea, were investigated by using rat intestinal enzymes and human Caco-2 cells. Regarding rat intestinal enzyme
Saber Abdelkader Saidi et al.
Heliyon, 8(12), e11954-e11954 (2022-12-09)
The study evaluated the phytochemical composition of Ephedra alata and its effects on α-amylase and lipase enzymes and diabetic-induced liver-kidney-testes toxicities to determine the anti-diabetic, anti-obesity, and anti-toxic potentials of the plant. Obesity was induced by a high-fat and fructose
Annabel Bijttebier et al.
Carbohydrate research, 345(2), 235-242 (2009-12-08)
Amylopectin fine structures were studied following limited hydrolysis of gelatinised waxy maize starch by amylases with a different level of inner chain attack (LICA). This was done by size exclusion chromatography as well as by debranching the (partially hydrolysed) amylopectin
Bjarte Aarmo Lund et al.
Molecules (Basel, Switzerland), 26(23) (2021-12-11)
The determination of the temperature dependence of enzyme catalysis has traditionally been a labourious undertaking. We have developed a new approach to the classical Arrhenius parameter estimation by fitting the change in velocity under a gradual change in temperature. The

Protokolle

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.

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