Anti-phospho-Tyrosine Hydroxylase (Ser40)

Tyrosine hydroxylase (TH, tyrosine 3-monooxygenase) is the eukaryotic enzyme that catalyzes the first, rate-limiting step in the biosynthesis of dopamine and other catecholamines from tyrosine. TH requires O2 and ferrous iron for the hydroxylation reaction it catalyzes. In mammals, TH is encoded by a single gene that is required for embryonic development and survival,2 full-length cDNA for this enzyme has been obtained for rat, mouse, bovine, Drosophila, macaque monkey, and human species. In all vertebrates, TH activity is closely regulated at many levels of expression, including gene transcription, RNA processing, stability of mRNA, feedback inhibition on enzyme, and protein kinase activation. The active tyrosine hydroxylase enzyme is a tetramer, with its active site located within its C-terminal region, where the physiological co-substrate binds. The N-terminus acts as a regulatory domain, and contains four serine residues, including Ser 19, Ser 31, and Ser40, that can be phosphorylated by protein kinase A (PKA), CaM kinase II (CaMKII), and protein kinase C (PKC). Ser40 is the major TH phosphorylation site of PKA and CaMKII in vertebrates.2,3 Phosporylation of TH at Ser40, and thus the synthesis of dopamine, has been observed to be influenced by many factors, including potassium ion concentration,4 activation of adenylyl cyclase,5 NMDA receptor activity,5 ERK1/2 activity,6,7 and the binding of 14-3-3 proteins. Applications: Suitable for use in ELISA, Western Blot, Immunofluorescence and Immunohistochemistry. Other applications not tested. Recommended Dilution: Western Blot: 1:1000 , Immunohistochemistry: 1:1000, Immunofluorescence: 1:1000, Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.