| Species : |
Human |
| Source : |
Mammalian Cells |
| Tag : |
His |
| Description : |
Pedptidylglycine αAmidatingMonooxygenase (PAM) catalyzes the Cterminal amidation that is required for thefunction of a number of peptide hormones. PAM possesses two enzymatic activitieson a single polypeptide chain, due to the presense of a peptidylglycine αhydroxylatingmonooxygenase (PHM) domain and a peptidylαhydroxyglycine αamidating lyase (PAL)domain. The Cterminal glycines of precursor peptides are hydroxylated at theglycine α carbon by the PHM activity in a reaction that requires ascorbate, thenthe PAL activity completes the amidation, releasing glyoxylate in the process.PAM is required for the biosynthesis of peptides such as Substance P, neuropeptideY, oxytocin, vasopressin, and calcitonin. PAM is highly expressed in tissues thatsynthesize bioactive peptides, such as the thyroid and pituitary glands. The enzymeis generally stored in secretory granules, but soluble secreted forms have beenobserved. Recombinant human PAM was expressed as a Cterminally truncated proteinlacking its transmembrane and cytosolic domains to facilitate its secretion. |
| Form : |
Lyophilized from a 0.2μm filtered solution in Tris and NaCl. |
| N-terminal Sequence : |
Phe21 |
| Molecular Weight : |
90 kDa |
| Activity : |
Measured by the conversionof DTyrValGly to DTyrValNH2. The specific activity is > 350 pmol/min/μg,as measured under the described conditions. See Activity Assay Protocol. |
| Purity : |
>95%, by SDSPAGEunder reducing conditions and visualized by Colloidal Coomassie® Blue stain at5 μg per lane. |
| Endotoxin Level : |
<1.0 EU per 1 μg ofthe protein by the LAL method. |
| Storage : |
Use a manual defrostfreezer and avoid repeated freeze-thaw cycles. 6 months from date of receipt,70 °C as supplied. 3 months, 70 °C under sterile conditions after opening. |
| OfficialSymbol : |
PAM |