As mentioned in the 'DESCRIPTION' section, this product is a lyophilized powder containing (NH4)2SO4, sodium citrate and sodium chloride. This product is not tested for purity. However, buffer salts are expected to be the bulk of the non-protein content.
A1031
α-Amylase from human saliva
Type XIII-A, lyophilized powder, 300-1,500 units/mg protein
Synonym(s):
1,4-α-D-Glucan-glucanohydrolase
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1000 UNITS
₩299,730
5000 UNITS
₩1,054,382
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1000 UNITS
₩299,730
5000 UNITS
₩1,054,382
About This Item
Recommended Products
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
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sustainability
Greener Alternative Product
UniProt accession no.
greener alternative category
storage temp.
−20°C
Gene Information
human ... AMY1A(276)
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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.[1]
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 [2]. α-Amylase from human saliva has been used to study the development of nutraceuticals, which may aid the treatment of diabetes and obesity [3].
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.[4]
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 powder containing (NH4)2SO4, sodium citrate and sodium chloride.
Other Notes
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
substrate
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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Certificates of Analysis (COA)
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Protocols
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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Hi, could you let me know what the remaining composition is when the product contains 5-15% protein? Thank you!
1 answer-
Helpful?
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Please let me know the storage temperature and storage period when it is dissolved in water
1 answer-
The stability of this material in solution has not been investigated. However, various sources suggest that solutions may be stored in working aliquots at -20°C for several months.
Helpful?
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What is the recommended method for dissolving alpha amylase obtained from human saliva, specifically A1031?
1 answer-
The recommended method is to dissolve the enzyme in 1mM calcium chloride (CaCl2).
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Could you please tell me the weight (mg or gram) of sample A1031?
1 answer-
This product is sold based on units of activity. The activity specification is 300 - 1500 U/mg. The unit per milligram value is reported in the lot-specific Certificate of Analysis and will range from 0.67 to 3.3 mg for the 1000 U pack size.
See the link below to review a sample Certificate:
https://www.sigmaaldrich.com/certificates/sapfs/PROD/sap/certificate_pdfs/COFA/Q14/A1031-1KU0000270112.pdfHelpful?
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