Reactivity | Hu, Mu, RtSpecies Glossary |
Applications | WB, Simple Western, IHC, ICC/IF |
Clonality | Polyclonal |
Host | Sheep |
Conjugate | Unconjugated |
Concentration | LYOPH |
Immunogen | E. coli-derived recombinant human Tyrosine Hydroxylase Ala278-Tyr401, predicted Accession # P07101 |
Specificity | Detects human, mouse and rat Tyrosine Hydroxylase in Western blots. |
Source | N/A |
Isotype | IgG |
Clonality | Polyclonal |
Host | Sheep |
Gene | TH |
Purity Statement | Antigen Affinity-purified |
Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
Dilutions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS. |
Preservative | No Preservative |
Concentration | LYOPH |
Reconstitution Instructions | Sterile PBS to a final concentration of 0.2 mg/mL. |
TH (Tyrosine 3-hydroxylase; also tyrosine 3-monooxygenase) is a 60-62 kDa member of the biopterin-dependent aromatic amino acid hydroxylase family of molecules. It is expressed by neurons of the dopamine and autonomic nervous system, plus the neuroendocrine cells of the adrenal medulla. TH is considered the rate limiting enzyme for catecholamine synthesis, and serves to catalyze the hydroxylation of L-tyrosine. It maintains stores of catecholamines following secretion, and its activity is regulated by targeted site phosphorylation. Human TH is 528 amino acids (aa) in length. It contains an N-terminal ACT domain (aa 69-190) that binds small molecules and regulates enzyme activity, and a C-terminal enzymatic region (aa 196-493). There are three significant utilized phosphorylation sites. Two at Ser31 and Ser40 increase enzyme activity, while phosphorylation at Ser19 promotes subsequent Ser40 phosphorylation. TH functions as a 240 kDa noncovalent homotetramer. There are four potential splice variants. One shows a deletion of aa 31-34, a second shows a deletion of aa 31-61, while a third contains a Met substitution for aa 1-34. A fourth isoform variant shows a deletion of aa 35-61. Over aa 278-401, human TH shares 94% aa sequence identity with mouse TH, a molecule that most closely resembles the fourth human isoform variant described above.
Secondary Antibodies |
Isotype Controls |
Successful Transplantation of Friedreich Ataxia Induced Pluripotent Stem Cell (iPSC)-Derived Sensory Neurons in Dorsal Root Ganglia of Adult Rodents Jamshed Arslan, Pharm D, PhD The dorsal root ganglia (DRG) are a collection of cell bodies of sensory nerves carrying sensory information – including nociception, mechanoreception and proprioception – from periphera... Read full blog post. |
The identification of dopaminergic neurons using Tyrosine Hydroxylase in Parkinson's research and LRRK2 Tyrosine hydroxylase (TH) is a crucial enzyme involved in the biosynthesis of dopamine, norepinephrine and epinephrine in the brain. Specifically, TH catalyzes the conversion of l-tyrosine to l-dihydroxyphenylalanine (l-dopa). The importance of t... Read full blog post. |
Tyrosine hydroxylase - a marker for dopaminergic neurons in the central nervous system Tyrosine hydroxylase is a member of the aromatic amino acid hydroxylase (AAAH) family. It is expressed throughout the central nervous system (CNS) and catalyzes the conversion of tyrosine to L-3,4-dihydroxyphenylalanine (L-DOPA), which can be, thr... Read full blog post. |
Tyrosine Hydroxylase - rate-limiting enzyme in catecholamine synthesis Catecholamines are tyrosine-derived hormones that are produced in the adrenal gland. They include epinephrine, norepinephrine, and dopamine and are used as neurotransmitters by the central and peripheral nervous system. The rate limiting enzyme in ... Read full blog post. |
A Big Guy for the Catecholamine Synthesis - Tyrosine hydroxylase (TH) In the synthesis pathway for the catecholamines - dopamine, epinephrine, and norepinephrine, tyrosine hydroxylase is the rate-limiting enzyme. Through alternative mRNA splicing, a wide molecular diversity of TH isoforms are generated that are tissue-s... Read full blog post. |
Tyrosine Hydroxylase Deficiencies and Neurodegeneration Tyrosine hydroxylase is the rate-limiting enzyme in the synthesis pathway of the catecholamines dopamine, epinephrine, and norepinephrine. Alternative mRNA splicing generates a wide molecular diversity of TH isoforms that are tissue specific and produ... Read full blog post. |
Tyrosine Hydroxylase Deficiency and Brain Disorders Tyrosine hydroxylase catalyzes the rate-limiting step in the biosynthesis of the catecholamines dopamine, norepinephrine, and epinephrine. A hallmark of Parkinson's disease is the loss of dopaminergic neurons in the substantia nigra. Mutations in cas... Read full blog post. |
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