alpha amylase/AMY2A Proteins, cDNA Clones Research Reagents

All alpha amylase/AMY2A reagents are produced in house and quality controlled, including 13 alpha amylase/AMY2A Gene, 3 alpha amylase/AMY2A Lysate, 3 alpha amylase/AMY2A Protein, 1 alpha amylase/AMY2A qPCR. All alpha amylase/AMY2A reagents are ready to use.

alpha amylase/AMY2A Protein (3)

    alpha amylase/AMY2A cDNA Clone (13)


    クローニングベクター cDNA 製品

    In lentiviral vector

    alpha amylase/AMY2A qPCR Primer (1)

    alpha amylase/AMY2A Lysate (3)

      alpha amylase/AMY2A の背景知識

      Alpha-amylase is the major form of amylase found in humans and other mammals. 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 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.

      alpha amylase/AMY2A の参考文献

      • Abe A, et al. (2005) Complexes of Thermoactinomyces vulgaris R-47 Alpha-amylase / AMY2A 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with alpha-(1,6) glycosidic linkages. FEBS J. 272(23):6145-53.
      • Aghajari, N, et al. (1998) Crystal structures of the psychrophilic Alpha-amylase / AMY2A from Alteromonas haloplanctis in its native form and complexed with an inhibitor. Protein Sci. 7(3): 564-72.
      • Ramasubbu, N, et al. (1996) Structure of Human Salivary -Amylase at 1.6 Resolution: Implications for its Role in the Oral Cavity. Acta Crystallographica Section D Biological Crystallography. 52(3):435-46.

      Note: Flag® is a registered trademark of Sigma Aldrich Biotechnology LP. It is used here for informational purposes only.