Anti-PAH Polyclonal Antibody for WB, ELISA - P00439

Core Product Specifications and Parameters

Biological Background: PAH Function and Localization

• PAH (phenylalanine-4-hydroxylase) is the key enzyme that catalyzes the hydroxylation of L-phenylalanine to L-tyrosine, a critical step in phenylalanine catabolism.
• It functions as an allosteric enzyme, regulated by its substrate and other metabolites to maintain appropriate tyrosine levels.
• PAH is a monooxygenase that requires iron as a cofactor for its catalytic activity.
• Mutations in the PAH gene are linked to phenylketonuria (PKU), a metabolic disorder characterized by elevated phenylalanine levels.
• The protein is subject to phosphorylation, which may modulate its activity in response to cellular signals.
• PAH is a member of the aromatic amino acid hydroxylase family and is a reference proteome component in proteomics studies.

Experimental Guidance and Technical Tips

• For Western blotting, a band around 52 kDa is expected; validate with positive and negative controls in the relevant sample system.
• ELISA performance may require optimization of coating antibody concentration and blocking conditions; consider using recombinant PAH protein as a standard.
• Cross-reactivity with rat has been observed; verify performance in your specific experimental models if using rat tissues or cells.
• The immunogen spans amino acids 110-452, excluding the N-terminal regulatory domain; this may affect detection of certain isoforms or processed forms.

CamelBio: Your One-Stop Sourcing Bridge

CamelBio connects diagnostic manufacturers, laboratories, and research institutes with high-quality IVD raw materials, technical services, and consulting—from concept to clinic. For studies on amino acid metabolism, phenylketonuria, or related enzymopathies, we supply validated antibody pairs and reagents, including this anti-PAH polyclonal antibody. We also support rare-target raw-material sourcing and bulk ancillary reagent procurement to accelerate your diagnostic development.