| Description : |
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 f centigradeusing, and can also be separated in testing by using specific mon centigradelonal antibodies. |
| Source : |
HEK293 |
| Species : |
Human |
| Tag : |
Fc |
| Predicted N Terminal : |
Gln 16 |
| Form : |
Lyophilized from sterile PBS, pH 7.4. Normally 5 %- 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. |
| Molecular Mass : |
The recombinant human AMY2B consists 732 amino acids and predicts a molecular mass of 82.4 kDa. |
| Protein length : |
Met1-Leu511 |
| Endotoxin : |
< 1.0 EU per μg protein as determined by the LAL method. |
| Purity : |
> 95 % as determined by SDS-PAGE. |
| Storage : |
Samples are stable for up to twelve months from date of receipt at-70 centigrade. Store it under sterile conditions at-20 centigrade to-80 centigrade. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
| Reconstitution : |
It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4℃ before opening to recover the entire contents. |
