Skip to Content
Merck
CN

A1031

α-Amylase from human saliva

greener alternative

Type XIII-A, lyophilized powder, 300-1,500 units/mg protein

Synonym(s):

1,4-α-D-Glucan-glucanohydrolase

Sign In to View Organizational & Contract Pricing.

Select a Size

Change View

About This Item

CAS Number:
UNSPSC Code:
12352204
eCl@ss:
32160410
EC Number:
232-565-6
NACRES:
NA.54
MDL number:
EC Number:
Specific activity:
300-1,500 units/mg protein
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist


type

Type XIII-A

Quality Level

form

lyophilized powder

specific activity

300-1,500 units/mg protein

composition

Protein, 5-15% biuret

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.

greener alternative category

storage temp.

−20°C

Gene Information

human ... AMY1A(276)

General description

Human α-amylase is made up of 496 amino acids in a single polypeptide chain, which is encrypted on chromosome 1. These are produced either in the salivary glands or the pancreas. The salivary and pancreatic α-amylases have homologous primary sequence but exhibit different cleavage patterns.
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. Product A1031 is from human saliva, is type IIA, and is supplied as a lyophilized powder. α-Amylase has been used in various plant studies, such as metabolism studies in Arabidopsis . α-Amylase from human saliva has been used to study the development of nutraceuticals, which may aid the treatment of diabetes and obesity .

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.

Physical form

Lyophilized powder containing (NH4)2SO4, sodium citrate and sodium chloride.

Other Notes

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


Still not finding the right product?

Explore all of our products under α-Amylase from human saliva


Hazard Classifications

Resp. Sens. 1

pictograms

Health hazard

signalword

Danger

hcodes

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

高风险级别生物产品--人源产品

This item has



Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library


Protocols

可根据此操作规程测定α-淀粉酶的活性。该α-淀粉酶酶促测定将会指导您完成整个过程及必要的计算。

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.


Lana Zupancic Cepic et al.
Oral diseases, 26(5), 1072-1080 (2020-03-04)
This study aimed to characterize surface properties such as roughness (Ra) and surface-free energy (SFE) of glazed and polished yttria-stabilized zirconia and to evaluate in vitro adherence of fungus Candida albicans and salivary bacteria, Staphylococcus epidermidis, mixed with C. albicans
Digestive enzyme inhibitors from grains as potential components of nutraceuticals.
D Piasecka-Kwiatkowska, et al.
J. Nutr. Sci. Vitaminol., 58, 217-220 (2012)
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



Global Trade Item Number

SKUGTIN
A1031-1KU04061833334690
A1031-5KU04061833334706