추천 제품
유형
Type XIII-A
Quality Level
형태
lyophilized powder
특이 활성도
300-1,500 units/mg protein
구성
Protein, 5-15% biuret
환경친화적 대안 제품 특성
Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
sustainability
Greener Alternative Product
UniProt 수납 번호
환경친화적 대안 카테고리
저장 온도
−20°C
유전자 정보
human ... AMY1A(276)
유사한 제품을 찾으십니까? 방문 제품 비교 안내
일반 설명
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.
애플리케이션
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 .
생화학적/생리학적 작용
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.
단위 정의
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.
물리적 형태
Lyophilized powder containing (NH4)2SO4, sodium citrate and sodium chloride.
기타 정보
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
신호어
Danger
유해 및 위험 성명서
예방조치 성명서
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
이미 열람한 고객
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
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
Priscila Brigide et al.
Food & function, 10(8), 4802-4810 (2019-07-19)
The present work evaluated the effect of different processes in relation to mineral content and its bioavailability, as well as the effect of phytate and oxalate contents in biofortified beans. The following treatments were evaluated: raw beans (RB), cooked and
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)
프로토콜
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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