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AMY2B  Proteína

All AMY2B Reagents

Anfitrión de expresión: Human Cells  
13575-H02H-20
13575-H02H-100
20 µg 
100 µg 
Add to Cart
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Anfitrión de expresión: Human Cells  
13575-H08H-20
13575-H08H-100
20 µg 
100 µg 
Add to Cart
  • Slide 1

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AMY2B Related Area

AMY2B Vías relacionadas

    AMY2B Resumen e información sobre la proteína

    AMY2B Fondo

    Actividad catalítica: Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.
    Cofactor: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; ; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};; Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250}; ; Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250};
    Estructura de subunidad: Monomer. {ECO:0000250}.
    Localización subcelular: Secreted {ECO:0000250}.
    Similitud de la secuencia: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
    General information above from UniProt

    Amylases are secreted proteins that hydrolyze 1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides, and thus catalyze the first step in digestion of dietary starch and glycogen. Alpha-amylase is the major form of amylase found in humans and other mammals. Alpha-amylase hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. Amylases is widely expressed and is most prominent in pancreatic juice and saliva, each of which has its own isoform of human α-amylase. They behave differently on isoelectric focusing, and can also be separated in testing by using specific monoclonal antibodies.

    AMY2B Nombre alternativo

    HXA,AMY2,AMY3, [homo-sapiens]
    AMY3,HXA, [Human]
    Amy-X,Amy2-2,mAmy2-1, [mouse]
    Amy-X,Amy2-2,mAmy2-1,OTTMUSG00000022462, [mus-musculus]

    AMY2B Estudios relacionados

  • Abe A. et al., 2005, FEBS J. 272 (23): 6145-53.
  • Aghajari N. et al., 1998, Protein Sci. 7 (3): 564-72.
  • Ramasubbu N. et al., 1996, Acta Crystallographica Section D Biological Crystallography. 52 (3): 435-46.
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