Analytical Data
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Gene name
GCH1
- Application
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Alternative Names
DYT5; GCH; GTP-CH-1; DYT5a; GTPCH1; Dopa-Responsive Dystonia
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P30793
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Expression Region
Ala16~Ser250
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Molecular Weight
32kDa
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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
GCH1 (GTP cyclohydrolase 1) is a key enzyme in the biosynthesis of tetrahydrobiopterin (BH4), an essential cofactor for the synthesis of neurotransmitters such as dopamine, and is involved in regulating nitric oxide production. Deficiencies in GCH1 activity can lead to a variety of clinical conditions, including hyperphenylalaninemia and neurometabolic disorders, which are characterized by neurological symptoms and other metabolic dysfunctions. Due to its critical role in both neurotransmitter synthesis and metabolic pathways, there has been considerable interest in the recombinant production of GCH1 for therapeutic applications and as a biochemical tool in research. Producing GCH1 as a recombinant protein allows for the exploration of its structural and functional properties, facilitating the development of potential treatments for related disorders. Advances in genetic engineering techniques have made it feasible to express GCH1 in various host systems, such as bacteria and yeast, enabling high-yield production and detailed characterizations of the enzyme. Understanding GCH1’s interactions and modulatory mechanisms could provide insights into its role in the central nervous system and its potential as a drug target. Additionally, studies involving recombinant GCH1 may contribute to the development of novel therapeutic strategies to enhance BH4 synthesis or increase its availability in conditions associated with GCH1 deficiency. Thus, research on recombinant GCH1 not only deepens our understanding of fundamental biochemical processes but also holds promise for innovating treatment pathways for metabolic and neurodegenerative diseases.
