Description_x000D_ General description_x000D_ The ALAD enzyme is composed of 8 identical subunits and catalyzes the condensation of 2 molecules of delta-aminolevulinate to form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins). ALAD catalyzes the second step in the porphyrin and heme biosynthetic pathway; zinc is essential for enzymatic activity. ALAD enzymatic activity is inhibited by lead and a defect in the ALAD structural gene can cause increased sensitivity to lead poisoning and acute hepatic porphyria. (provided by RefSeq)_x000D_ Immunogen_x000D_ ALAD (NP_000022.2, 1 a.a. ~ 339 a.a) full-length human protein._x000D_ Sequence_x000D_ MPLCPLAHAMQPQSVLHSGYFHPLLRAWQTATTTLNASNLIYPIFVTDVPDDIQPITSLPGVARYGVKRLEEMLRPLVEEGLRCVLIFGVPSRVPKDERGSAADSEESPAIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSENGAFRAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKEALMAHGLGNRVSVMSYSAKFASCFYGPFRDAAKSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADMLMVKPGMPYLDIVREVKDKHPDLPLAVYHVSGEFAMLWHGAQAGAFDLKAAVLEAMTAFRRAGADIIITYYTPQLLQWLKEE_x000D_ Application_x000D_ Anti-ALAD antibody produced in mouse is suitable for western blot application._x000D_ Physical form_x000D_ Solution in phosphate buffered saline, pH 7.4_x000D_ Biochem/physiol Actions_x000D_ The cytosolic ALAD (δ-aminolevulinic acid dehydratase) plays a vital role in the heme biosynthetic pathway. It facilitates the second step, which is a condensation reaction of 5-aminolevulinic acid and forms a monopyrrole termed as porphobilinogen. It is one of the main targets of lead toxicity. Lead replaces zinc present in ALAD, leading to inactivation of the enzyme. Deficiency in ALAD causes ALAD deficiency porphyria (ADP).