Recombinant human Tryptophan Hydroxylase/TPH protein (Active) is a Human Fragment protein, in the 105 to 420 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, FuncS.
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Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Oxidizes L-tryptophan to 5-hydroxy-l-tryptophan in the rate-determining step of serotonin biosynthesis.
TPH, TPRH, TRPH, TPH1, Tryptophan 5-hydroxylase 1, Tryptophan 5-monooxygenase 1
Recombinant human Tryptophan Hydroxylase/TPH protein (Active) is a Human Fragment protein, in the 105 to 420 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, FuncS.
pH: 8
Preservative: 1.16% Imidazole
Constituents: 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.63% Tris HCl, 0.05% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.04% Sorbitan monolaurate, ethoxylated, 0.02% Potassium chloride
Affinity purified.
Oxidizes L-tryptophan to 5-hydroxy-l-tryptophan in the rate-determining step of serotonin biosynthesis.
Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.
Ubiquitinated, leading to its degradation by the proteasome. Ubiquitinated is triggered by phosphorylation.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
This product was previously labelled as Tryptophan Hydroxylase
Tryptophan Hydroxylase (TPH) is an enzyme that plays a critical mechanical role in the body. It is sometimes known as TPH or anti TPH. The enzyme catalyzes the conversion of tryptophan to 5-hydroxytryptophan the first and rate-limiting step in the biosynthesis of serotonin. The molecular mass of TPH is approximately 55 kDa. TPH has two isoforms TPH1 and TPH2 which are expressed in different tissues. TPH1 is mainly found in peripheral tissues such as the gut pineal gland and thymus while TPH2 is expressed in the central nervous system particularly in the raphe nuclei of the brainstem.
Tryptophan hydroxylase serves an important role in serotonin production which impacts mood regulation sleep and other functions. TPH operates primarily as a homotetramer and requires biopterin oxygen and iron for its activity. Serotonin synthesized as a result acts as a neurotransmitter and hormone influencing various physiological processes. The differential expression of TPH1 and TPH2 allows for compartmentalized regulation of serotonin synthesis addressing both peripheral and central nervous system needs.
TPH is central in the serotonin biosynthetic pathway a critical pathway for neuromodulation. It converts tryptophan into 5-hydroxytryptophan which is then decarboxylated to serotonin. TPH's function connects closely with other proteins in these pathways such as Aromatic L-amino acid decarboxylase which further processes 5-hydroxytryptophan into serotonin. This integration within the serotonin pathway highlights its importance in maintaining serotonin levels and consequently normal neurological function.
Tryptophan hydroxylase has associations with mood disorders and irritable bowel syndrome (IBS). Altered TPH activity may lead to disruptions in serotonin levels influencing development and progression of these conditions. Studies often link TPH2 with depression and anxiety due to its central neural expression and role in serotonin synthesis. Meanwhile TPH1 expressed in peripheral tissues has connections to IBS where serotonin significantly affects gut motility and sensitivity. The relationship between these disorders and TPH offers insights into therapeutic targets to modulate serotonin levels for treatment strategies.
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Activity assay using ab206448
6-20% SDS-PAGE stained with Coomassie Blue.
Lane 1: ab206448 (5 μg)
Lane 2: Protein Marker
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