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Indirect immunofluorescence staining of rat retinal dopaminergic neurons using Zymed Rb anti-phospho-Tyrosine Hydroxylase (Ser31) (Cat. No. 36-9900). Image courtesy of Paul Witkovsky, PhD, Dept. of Ophthalmology, New York University School of Medicine.
|Tested species reactivity||Rat|
|Published species reactivity||Rat , Mouse|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic phospho peptide derived from a region of the rat tyrosine hydroxylase (TH) protein surrounding the phosphorylated Ser31 residue.|
|Storage buffer||0.01M HEPES, pH 7.5, with 100µg/ml BSA, 50% glycerol, 0.15M NaCl|
|Tested Applications||Dilution *|
|Western Blot (WB)||1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
|Western Blot (WB)||See 3 publications below|
Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the synthesis of the catecholamine neurotransmitters (dopamine, epinephrine, and norepinephrine). It is responsible for the conversion of L-tyrosine to L-dopa in the catecholamine synthesis pathway
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Progesterone decreases tyrosine hydroxylase phosphorylation state and increases protein phosphatase 2A activity in the stalk-median eminence on proestrous afternoon.
||Liu B,Arbogast LA||The Journal of endocrinology (204:209)||2010|
Phosphorylation state of tyrosine hydroxylase in the stalk-median eminence is decreased by progesterone in cycling female rats.
36-9900 was used in western blot to study the role of tyrosine hydroxylase in the stalk-median eminence of female rats.
|Liu B,Arbogast LA||Endocrinology (149:1462)||2008|
Regulation of dopaminergic transmission and cocaine reward by the Clock gene.
||McClung CA,Sidiropoulou K,Vitaterna M,Takahashi JS,White FJ,Cooper DC,Nestler EJ||Proceedings of the National Academy of Sciences of the United States of America (102:9377)||2005|
tyrosine 3-hydroxylase, tyrosine 3-monooxygenase, EC 188.8.131.52, TH isoform 3, TH isoform a, TH-4, TY3H, TYH, Tyrosine 3-monooxygenase, tyrosine hydroxylase