Phospho-Tyrosine Hydroxylase (Ser31) Antibody #3370
- WB
- IP
Supporting Data
| REACTIVITY | R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 55-60 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Phospho-Tyrosine Hydroxylase (Ser31) Antibody detects endogenous levels of tyrosine hydroxylase only when phosphorylated at Ser31.
Species Reactivity:
Rat
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Mouse
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to the sequence surrounding Ser31 of mouse tyrosine hydroxylase. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the synthesis of the neurotransmitter dopamine and other catecholamines. TH functions as a tetramer, with each subunit composed of a regulatory and catalytic domain, and exists in several different isoforms (1,2). This enzyme is required for embryonic development since TH knockout mice die before or at birth (3). Levels of transcription, translation and post-translational modification regulate TH activity. The amino-terminal regulatory domain contains three serine residues: Ser9, Ser31, and Ser40. Phosphorylation at Ser40 by PKA positively regulates the catalytic activity of TH (4-6). Phosphorylation at Ser31 by CDK5 also increases the catalytic activity of TH through stabilization of TH protein levels (7-9).
- Kumer, S.C. and Vrana, K.E. (1996) J Neurochem 67, 443-62.
- Bodeau-Péan, S. et al. (1999) J Biol Chem 274, 3469-75.
- Kobayashi, K. et al. (1995) J Biol Chem 270, 27235-43.
- Lew, J.Y. et al. (1999) Mol Pharmacol 55, 202-9.
- Vié, A. et al. (1999) J Biol Chem 274, 16788-95.
- Lindgren, N. et al. (2000) J Neurochem 74, 2470-7.
- Moy, L.Y. and Tsai, L.H. (2004) J Biol Chem 279, 54487-93.
- Lehmann, I.T. et al. (2006) J Biol Chem 281, 17644-51.
- Saraf, A. et al. (2007) J Biol Chem 282, 573-80.
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