Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Tyrosine Hydroxylase (E2L6M) Horse Chimeric mAb #90818
Filter:
- IF
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | |
| Source/Isotype | Horse Chimera IgG4 |
Application Key:
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Description
This Cell Signaling Technology® antibody retains the antigen-binding Fab regions of the original parent host sequence from which it is engineered. This antibody is expected to exhibit the same species cross-reactivity as Tyrosine Hydroxylase (E2L6M) Rabbit mAb #58844.
Product Usage Information
| Application | Dilution |
|---|---|
| Immunofluorescence (Frozen) | 1:50 - 1:200 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Tyrosine Hydroxylase (E2L6M) Horse Chimeric mAb recognizes endogenous levels of total tyrosine hydroxylase protein.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
This recombinant chimeric antibody is engineered from Tyrosine Hydroxylase (E2L6M) Rabbit mAb #58844 according to animal-free protocols. The chimeric antibody retains its antigen-binding Fab regions from the original rabbit monoclonal antibody but contains a horse-derived Fc domain. When multiplexing, Fc-directed rabbit secondaries are required to detect rabbit-host primary antibodies.
The parent antibody, Tyrosine Hydroxylase (E2L6M) Rabbit mAb #58844, is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human tyrosine hydroxylase protein.
The parent antibody, Tyrosine Hydroxylase (E2L6M) Rabbit mAb #58844, 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.
限制使用
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For Research Use Only. Not for Use in Diagnostic Procedures.
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