Species : |
Mouse |
Source : |
HEK293 |
Tag : |
DDK&Myc |
Description : |
Bifunctional enzyme that catalyzes the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides. Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme. The first step, catalyzed by peptidyl alpha-hydroxylating monoxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate. The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc-dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate. Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (Probable). |
Molecular Mass : |
109.3 kDa |
Purity : |
> 80% as determined by SDS-PAGE and Coomassie blue staining |
Stability : |
Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles. |
Storage : |
Store at -80 centigrade after receiving vials. |
Concentration : |
>50 μg/mL as determined by microplate BCA method |
Storage Buffer : |
25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10% glycerol. |