Analytical Data
-
Gene name
TPH2
- Application
-
Alternative Names
Neuronal tryptophan hydroxylase Tryptophan 5-monooxygenase 2
-
Species
Human
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8IWU9
-
Expression Region
1-490aa
-
Molecular Weight
60.1 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
TPH2 (Tryptophan Hydroxylase 2) is a critical enzyme involved in the biosynthesis of serotonin, a neurotransmitter vital for regulating mood, anxiety, and various neurological functions. Research into TPH2 has gained momentum due to its significant role in psychiatric disorders such as depression, anxiety disorders, and schizophrenia, where dysregulation of serotonin signaling is often implicated. Understanding the structure and function of TPH2 is crucial for developing therapeutic strategies aimed at restoring serotonin levels in the brain. Recombinant TPH2 proteins have been produced for in vitro studies to elucidate the enzyme's biochemical properties, regulatory mechanisms, and the effects of genetic variations on its activity. These studies have highlighted the importance of post-translational modifications and the enzyme's interaction with various cofactors. Moreover, by employing techniques such as site-directed mutagenesis and X-ray crystallography, researchers can investigate how specific mutations influence TPH2 function and contribute to the pathophysiology of mood disorders. This research is essential not only for advancing our understanding of serotonin metabolism but also for fostering the development of novel antidepressant therapies that target TPH2 and its related pathways. As a result, TPH2 remains a promising focus of biochemical and pharmacological research, with the potential to unlock new avenues for treating serious mental health conditions.
