Tyrosine Hydroxylase (E2L6M) Rabbit mAb (BSA and Azide Free) #81242
- WB
- IHC
- IF
- F
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 55-60 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
- IF-Immunofluorescence
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
This product is the carrier-free version of product #58844. All data were generated using the same antibody clone in the standard formulation which contains BSA and glycerol.
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN, or CUT&Tag assays. If you require a carrier-free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
Formulation
For standard formulation of this product see product #58844.
Storage
Specificity / Sensitivity
Tyrosine Hydroxylase (E2L6M) Rabbit mAb (BSA and Azide Free) recognizes endogenous levels of total tyrosine hydroxylase protein.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human tyrosine hydroxylase protein.
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.
Limited Uses
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