Sequentially cleaves N-terminal amino acids except E, D, and X-P.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris, 150mM NaCl, 5μM ZnSO4, pH8.0.
Endotoxin
Less than 0.1EU/μg of rAeromonas Aminopeptidase as determined by LAL method.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer to a concentration of 0.1-1.0mg/ml. Stock solutions should be apportioned into working aliquots and stored at ≤-20℃. Further dilutions should be made in appropriate buffered solutions.
Category
Enzymes
Background
Aminopeptidases catalyze the cleavage of amino acids from the amino terminus of protein or peptide substrates. They are widely distributed throughout the animal and plant kingdoms and are found in many subcellular organelles, in cytoplasm and as membrane components. Some aminopeptidases are monomeric and others are assemblies of relatively high mass (50kDa) subunits. Aminopeptidases play an important role in most diseases and biological processes including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Recombinant Aeromonas Aminopeptidase is a 31.4kDa protein containing 291 amino acid residues.