Rhesus AMY2A / Alpha-amylase Protein (Fc Tag)

AMY2A,AMY2B

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Catalog Number	P90012-C02H
Organism Species	Rhesus
Host	Human Cells
Synonyms	AMY2A,AMY2B
Molecular Weight	The recombinant rhesus AMY2A comprises 737 amino acids and has a calculated molecular mass of 82.8 KDa.
predicted N	Gln 16
SDS-PAGE
Purity	> 90 % as determined by SDS-PAGE
Protein Construction	A DNA sequence encoding the rhesus AMY2A (H9EX43) (Met1-Leu511) was expressed with the Fc region of human IgG1 at the C-terminus.
Bio-activity
Research Area
Formulation	Lyophilized from sterile PBS, pH 7.4. 1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background	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.
Reference	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.