Alternative NamesTH; Tyrosine hydroxylase; Tyrosine 3-monooxygenase; L-tyrosine hydroxylase; Tyrosine 3-hydroxylase
Application(s)IHC-Frozen
Antibody HostRabbit
Antibody TypePolyclonal
SpecificityIHC on brain shows a pattern of staining specific for TH containing neurons. This antibody is known to react with rat, mouse and guinea pig. Cross reactivity with other species has not yet been tested.
Species ReactivityGuinea Pig, Human, Mouse, Rat
Immunogen DescriptionA synthetic peptide (PRFIGRRQSLIEDARK) as part of human Tyrosine Hydroxylase (63-78) conjugated to KLH has been used as the immunogen. The peptide is homologous with the corresponding sequence derived from TH protein in rat (31-47).
Application DetailsIHC. A concentration of 4-10 µg/mL is recommended for this application. This is a superb antibody for detection of tyrosine hydroxylase containing neurons exhibiting an intense labelling with a negligible background. This antiserum has proven extremely useful for staining of catecholaminergic neurons. It stains nicely and intensely dendritic processes and fine nerve terminals. We recommend mouse or rat brain containing catecholaminergic neurons as a positive control for this antibody, for example brain stem or striatum. Western blotting: A concentration of 5-15 µg/mL is recommended.Biosensis recommends optimal dilutions/concentrations should be determined by the end user.
TargetTyrosine Hydroxylase (TH)
SpecificityIHC on brain shows a pattern of staining specific for TH containing neurons. This antibody is known to react with rat, mouse and guinea pig. Cross reactivity with other species has not yet been tested.
Target Host SpeciesHuman
Species ReactivityGuinea Pig, Human, Mouse, Rat
Antibody HostRabbit
Antibody TypePolyclonal
Antibody IsotypeIgG
ConjugateUnconjugated
Immunogen DescriptionA synthetic peptide (PRFIGRRQSLIEDARK) as part of human Tyrosine Hydroxylase (63-78) conjugated to KLH has been used as the immunogen. The peptide is homologous with the corresponding sequence derived from TH protein in rat (31-47).
Purity DescriptionProtein G purified
FormatLyophilized from PBS, pH 7.4, without preservatives.
Reconstitution InstructionsSpin vial briefly before opening. Reconstitute in 500 µL sterile-filtered 1X PBS, pH 7.2-7.6. Centrifuge to remove any insoluble material.
Storage InstructionsAfter reconstitution keep aliquots at -20°C for a higher stability, and at 2-8°C with an appropriate antibacterial agent. Avoid repetitive freeze/thaw cycles.
Batch NumberPlease see item label.
Expiration Date12 months after date of receipt (unopened vial).
Alternative NamesTH; Tyrosine hydroxylase; Tyrosine 3-monooxygenase; L-tyrosine hydroxylase; Tyrosine 3-hydroxylase
Scientific BackgroundTyrosine hydroxylase (TH) is the rate-limiting enzyme in the synthesis of the catecholamines dopamine, epinephrine and norepinephrine. Therefore the regulation of the TH enzyme represents the central means for controlling the synthesis of these important catecholamines. FUNCTION: Plays an important role in the physiology of adrenergic neurons. CATALYTIC ACTIVITY: L-tyrosine + tetrahydrobiopterin + O2 = 3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin. COFACTOR: Fe(2+) ion. ENZYME REGULATION: Phosphorylation leads to an increase in the catalytic activity. PATHWAY: Catecholamine biosynthesis; first step. SUBUNIT: Homotetramer. PTM: In vitro, phosphorylation of Ser-19 increases the rate of Ser-40 phosphorylation, which results in enzyme opening and activation. SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid hydroxylase family. The presence of different DNA sequences at the TH locus confers susceptibility to various disorders of the brain including manic-depression and schizophrenia. Parkinson's disease is also considered a TH deficiency as low dopamine levels are a consistent neurochemical abnormality.
Specific ReferencesPierre S.R., Lemmens M.A., Figueiredo-Pereira M.E. (2009) Subchronic infusion of the product of inflammation prostaglandin J2 models sporadic Parkinson's disease in mice J Neuroinflammation. Jul 25;6:18 Takeoka A. et al (2010) Noradrenergic innervation of the rat spinal cord caudal to a complete spinal cord transection: effects of olfactory ensheathing glia J Exp Neurol. 2010 Mar;222(1):59-69. Brown R.E. et al (2008) Characterization of GABAergic neurons in rapid-eye-movement sleep controlling regions of the brainstem reticular formation in GAD67-green fluorescent protein knock-in mice. Eur J Neurosci. 2008 Jan;27(2):352-63. Bisem NJ et al (2012) Mapping of FGF1 in the Medulla Oblongata of Macaca fascicularis. Acta Histochem Cytochem. 2012 Dec 26;45(6):325-34.
General ReferencesMallett, J. Trends in Pharmacological Science. 17(4): 129-135, 1996. Haavik, J. et al. Mol. Neurobiology 16(3) :285-309, 199 Lewis DA, et al, Neuroscience 54: 477, 1993 Kumer S.C. et al. Journal of Neurochemistry, 67(2) :443-462, 199 Haycock, J. Anal. Biochemistry 181: 259-266, 198 Haycock, J. Anal. Biochemistry 208: 397-399, 199 Renfroe, J.B., et al. Brain Res. Bull. 13: 109-126, 198 Xu, Z et a.l Neurosci. 82(3): 727, 1998