|Calculated MW||60 KDa|
|Other Names||Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase, TH, Th|
|Target/Specificity||Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser31 conjugated to KLH.|
|Format||Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns.|
|Antibody Specificity||Specific for the ~60k tyrosine hydroxylase protein phosphorylated atSer31.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Phospho-Ser31 Tyrosine Hydroxylase Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
email@example.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the synthesis of the catecholamines dopamine and norepinephrine. TH antibodies can therefore be used as markers for dopaminergic and noradrenergic neurons in a variety of applications including depression, schizophrenia, Parkinson’s disease and drug abuse (Kish et al., 2001; Zhu et al., 2000; Zhu et al., 1999). TH antibodies can also be used to explore basic mechanisms of dopamine and norepinephrine signaling (Witkovsky et al., 2000; Salvatore et al., 2001; Dunkley et al., 2004). The activity of TH is also regulated by phosphorylation (Haycock et al., 1982; Haycock et al., 1992; Jedynak et al., 2002). Phospho-specific antibodies for the phosphorylation sites on TH can be used to great effect in studying this regulation and in identifying the cells in which TH phosphorylation occurs.
Dunkley PR, Bobrovskaya L, Graham ME, Von Nagy-Felsobuki EI, Dickson PW (2004) Tyrosine hydroxylase phosphorylation: regulation and consequences. J Neurochem 91:1025-1043.
Haycock JW, Ahn NG, Cobb MH, Krebs EG (1992) ERK1 and ERK2, two microtubule-associated protein 2 kinases, mediate the phosphorylation of tyrosine hydroxylase at serine-31 in situ. Proc Natl Acad Sci (USA) 89:2365-2369.
Haycock JW, Bennett WF, George RJ, Waymire JC (1982) Multiple site phosphorylation of tyrosine hydroxylase. Differential regulation in situ by a 8-bromo-cAMP and acetylcholine. J Biol Chem 257:13699-13703.
Jedynak JP, Ali SF, Haycock JW, Hope BT (2002) Acute administration of cocaine regulates the phosphorylation of serine-19,-31 and-40 in tyrosine hydroxylase. J Neurochem 82:382-388.
Kish SJ, Kalasinsky KS, Derkach P, Schmunk GA, Guttman M, Ang L, Adams V, Furukawa Y, Haycock JW (2001) Striatal dopaminergic and serotonergic markers in human heroin users. Neuropsychopharmacology 24:561-567.
Salvatore MF, Waymire JC, Haycock JW (2001) Depolarization-stimulated catecholamine biosynthesis: involvement of protein kinases and tyrosine hydroxylase phosphorylation sites in situ. J Neurochem 79:349-360.
Witkovsky P, Gabriel R, Haycock JW, Meller E (2000) Influence of light and neural circuitry on tyrosine hydroxylase phosphorylation in the rat retina. J Chem Neuroanat 19:105-116.
Zhu MY, Klimek V, Haycock JW, Ordway GA (2000) Quantitation of tyrosine hydroxylase protein in the locus coeruleus from postmortem human brain. J Neurosci Meth 99:37-44.
Zhu MY, Klimek V, Dilley GE, Haycock JW, Stockmeier C, Overholser JC, Meltzer HY, Ordway GA (1999) Elevated levels of tyrosine hydroxylase in the locus coeruleus in major depression. Biol Psychiatry 46:1275-1286.
If you have used an Abgent product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at firstname.lastname@example.org.