This enzyme catalyzes the hydroxylation of L-phenylalanine to L-tyrosine, a critical step in the metabolic pathway of phenylalanine. Using molecular oxygen and tetrahydrobiopterin as cofactors, it introduces a hydroxyl group to the aromatic ring of phenylalanine, converting it into tyrosine. This reaction is essential for the biosynthesis of several neurotransmitters, including dopamine, norepinephrine, and epinephrine, as tyrosine serves as their precursor. Additionally, this process plays a pivotal role in protein metabolism and the regulation of phenylalanine levels in the body, preventing toxic accumulation that can lead to disorders such as phenylketonuria.
| Product Name | Recombinant Human Phenylalanine-4-Hydroxylase (PAH) |
| Accession | P00439 |
| Purity | Greater than 90% as determined by SDS-PAGE. |
| Host Species | Human |
| Gene | PAH |
| Source | E.coli |
| Protein Expression Range | 2-452aa |
| Tag | Tag-Free |
| Molecular Mass | 51.9 kDa |
| Form | Liquid or Lyophilized powder |
| Buffer | Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
| Storage | 1. Store at -20¡«C/-80¡«C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4¡«C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20¡«C/-80¡«C. Protein in lyophilized powder form is stable for up to 12 months at -20¡«C/-80¡«C. |
| Notes | 1 |
