PCBD1 Antibody / Pterin-4 alpha-carbinolamine dehydratase, 100 ug

PCBD1 antibody detects Pterin-4 alpha-carbinolamine dehydratase, a bifunctional enzyme that plays a role in tetrahydrobiopterin (BH4) regeneration and acts as a dimerization cofactor for hepatocyte nuclear factor 1 alpha (HNF1A). Encoded by the PCBD1 gene on chromosome 10q22.1, this protein contributes to phenylalanine, tyrosine, and tryptophan hydroxylation by recycling BH4, an essential cofactor for aromatic amino acid hydroxylases. PCBD1 thereby supports neurotransmitter biosynthesis and amino acid metabolism while also functioning in transcriptional regulation.

In its enzymatic role, PCBD1 catalyzes the dehydration of pterin-4 alpha-carbinolamine to quinonoid dihydrobiopterin, a step required for BH4 cofactor regeneration. Independently, as a dimerization cofactor, it stabilizes the DNA-binding form of HNF1A, influencing transcription of genes involved in glucose metabolism and hepatic differentiation. This dual functionality links metabolic and transcriptional control mechanisms within hepatocytes, endocrine tissues, and the central nervous system.

The PCBD1 antibody is widely used in enzymology, metabolic, and transcriptional biology research to study BH4 metabolism, amino acid hydroxylation, and HNF1A-dependent transcription. Western blot analysis identifies a 12 kilodalton band corresponding to PCBD1, while immunofluorescence reveals cytoplasmic and nuclear localization depending on cellular context. This antibody supports the investigation of enzyme regulation and transcriptional cofactor dynamics.

Mutations in PCBD1 cause hyperphenylalaninemia and transient neonatal diabetes due to impaired cofactor recycling and altered HNF1A transcriptional activity. The PCBD1 antibody is an essential reagent for exploring metabolic diseases, neurotransmitter synthesis, and transcriptional regulation. NSJ Bioreagents provides this antibody validated for its applications, ensuring accuracy in studies of enzymatic and regulatory networks.