Anti-PAH Antibody Picoband® Fluoro550 Conjugated

Phenylalanine hydroxylase (PAH) is an enzyme that catalyzes the hydroxylation of the aromatic side-chain of phenylalanine to generate tyrosine. It is one of three members of the biopterin-dependent aromatic amino acid hydroxylases, a class of monooxygenase that uses tetrahydrobiopterin (BH4, a pteridine cofactor) and a non-heme iron for catalysis. Deficiency of this enzyme activity results in the autosomal recessive disorder phenylketonuria.

E. coli-derived human PAH recombinant protein (Position: R71-H208) . Human PAH shares 89.1% and 88.4% amino acid (aa) sequence identity with mouse and rat PAH, respectively.

Receptor that mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. OxLDL is a marker of atherosclerosis that induces vascular endothelial cell activation and dysfunction, resulting in pro-inflammatory responses, pro-oxidative conditions and apoptosis. Its association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro-atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. In addition to binding oxLDL, it acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. Also involved in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation. Also acts as a receptor for advanced glycation end (AGE) products, activated platelets, monocytes, apoptotic cells and both Gram-negative and Gram-positive bacteria.

1. Fitzpatrick PF (1999) . Tetrahydropterin-dependent amino acid hydroxylases. Annual Review of Biochemistry. 68: 355–81. 2. Kaufman S (Feb 1958) . A new cofactor required for the enzymatic conversion of phenylalanine to tyrosine. The Journal of Biological Chemistry. 230 (2) : 931–9.