To ensure stability until the recommended retest date printed on the lot specific certificate of analysis, A1031 should be maintained at -20C after receipt. Transport conditions may differ from the recommended long-term storage conditions.
https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/marketing/global/documents/232/426/storage-transport-conditions-ms.pdf
A1031
α-Amylase from human saliva
Type XIII-A, lyophilized powder, 300-1,500 units/mg protein
Synonyma:
1,4-α-D-Glucan-glucanohydrolase
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Vybrat velikost
1000 UNITS
3 810,00 Kč
5000 UNITS
13 800,00 Kč
3 810,00 Kč
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O této položce
Číslo CAS:
UNSPSC Code:
12352204
eCl@ss:
32160410
EC Number:
232-565-6
NACRES:
NA.54
MDL number:
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Dovolte nám, abychom vám pomohliNázev produktu
α-Amylase from human saliva, Type XIII-A, lyophilized powder, 300-1,500 units/mg protein
type
Type XIII-A
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
Quality Level
Gene Information
human ... AMY1A(276)
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Související kategorie
1 of 4
Tato položka | A0521 | 10069 | 10070 |
|---|---|---|---|
| specific activity 300-1,500 units/mg protein | specific activity 1,000-3,000 units/mg protein | specific activity ~380 U/mg | specific activity ~50 U/mg |
| Gene Information human ... AMY1A(276) | Gene Information human ... AMY1A(276) | Gene Information - | Gene Information - |
| form lyophilized powder | form lyophilized powder | form powder | form powder |
| UniProt accession no. | UniProt accession no. | UniProt accession no. - | UniProt accession no. - |
| storage temp. −20°C | storage temp. −20°C | storage temp. 2-8°C | storage temp. 2-8°C |
| Quality Level 200 | Quality Level 200 | Quality Level 100 | Quality Level 100 |
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 [1]. α-Amylase from human saliva has been used to study the development of nutraceuticals, which may aid the treatment of diabetes and obesity [2].
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.[3]
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.[4]
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.
Other Notes
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
Physical form
Lyophilized powder containing (NH4)2SO4, sodium citrate and sodium chloride.
used together
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Skladovací třída
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Vyberte jednu z posledních verzí:
Již tento produkt vlastníte?
Dokumenty související s produkty, které jste v minulosti zakoupili, byly za účelem usnadnění shromážděny ve vaší Knihovně dokumentů.
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
Aleix Lluansí et al.
Frontiers in microbiology, 12, 716307-716307 (2021-10-29)
Inflammatory bowel disease (IBD), including its two main categories (Crohn's disease and ulcerative colitis), has been linked both to gut microbiota and to diet. Bread is a daily food that has a potential capacity as a prebiotic. Our aim was
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
Camila Gabriel Kato-Schwartz et al.
Food research international (Ottawa, Ont.), 137, 109462-109462 (2020-11-26)
A practical approach to control glycemia in diabetes is to use plant natural products that delay hydrolysis of complex sugars and promote the diminution of the release of glucosyl units into the blood plasma. Polyphenolics have been described as being
Protokoly
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.
Související obsah
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Can this be stored at room temperature until it is reconstituted or does it always need to be kept at -20C?
1 answer-
Helpful?
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Quanti mg di enzima sono contenuti in una confezione?
1 answer-
This product is sold by units and vial content will vary from lot to lot. The minimum activity of this enzyme is 300 units per milligram. The following values indicate the least amounts that will be present in each pack size:
1KU~ 3.3mg
5KU~16.6 mgThe exact specific activity will be listed on the lot specific Certificate of Analysis. Please see the link below to view a Certificate of Analysis: https://www.sigmaaldrich.com/product/sigma/a1031#product-documentation
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Considering the wide range of activity range, how can I be sure of the enzyme activity of the specific batch that I receive?
1 answer-
The protein content and enzymatic activity are determined on a lot to lot basis. Each value is reported in the specific Certificate of Analysis. The protein content range is 5 - 15% and the enzymatic activity range is 300 - 1500 units per milligram protein. A review of recent lots indicates typical protein concentrations of 7 - 13% and activities of 1350 - 1450 units per milligram protein. Please see the link below to review a sample or lot specific Certificate:
https://www.sigmaaldrich.com/product/sigma/a1031#product-documentationHelpful?
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¿Cómo se reconstituye la enzima al venir liofilizada? ¿Qué tasa de actividad tiene?
1 answer-
For assay purposes, this enzyme is reconstituted in water at 1 u/mL. This material is also soluble in 1 mM Calcium Chloride. 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. Please see the link below to review a sample or lot specific Certificate:
https://www.sigmaaldrich.com/product/sigma/a1031#product-documentationHelpful?
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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-
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.
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).
Helpful?
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