Analytical Data
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Gene name
Tph1
- Application
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Alternative Names
Tryptophan 5-monooxygenase 1
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Species
Mouse
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P17532
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Expression Region
1-447aa
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Molecular Weight
67.3 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
Tph1, or tryptophan hydroxylase 1, is a pivotal enzyme in the biosynthesis of serotonin, a neurotransmitter that plays a crucial role in mood regulation, appetite, and various physiological functions. The study of Tph1 has garnered considerable attention due to its implications in neuropsychiatric disorders, including depression, anxiety, and schizophrenia. Researchers have focused on the recombinant expression of Tph1 to better understand its structure, function, and regulation. By producing recombinant Tph1 in model systems, scientists can investigate the enzyme's catalytic mechanisms and interactions with various cofactors and substrates. Furthermore, this research has the potential to uncover novel therapeutic targets for drug development, given the enzyme's central role in serotonin production. The ability to manipulate Tph1 and its pathways might lead to innovative treatments for serotonin-related conditions, thus addressing a significant gap in current psychiatric care. Overall, the exploration of Tph1 recombinant protein is a promising avenue that bridges biochemistry and clinical applications, facilitating a deeper understanding of serotonin's diverse roles in health and disease.
