Analytical Data
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Gene name
GCHFR
- Application
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Alternative Names
GCHFR；GFRP;GTP cyclohydrolase 1 feedback regulatory Protein
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P30047
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Expression Region
1-84aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMPYLLISTQIRMEVGPTMVGDEQSDPE LMQHLGASKRRALGNNFYEYYVDDPPRIVLDKLERRGFRVLSMTGVGQTL VWCLHKE
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Molecular Weight
12 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
GCHFR (GTP cyclohydrolase I Feedback Regulator) is a crucial enzyme involved in the biosynthesis of tetrahydrobiopterin (BH4), an essential cofactor for the production of several neurotransmitters, including dopamine, serotonin, and norepinephrine. The regulation of GCHFR activity is pivotal for maintaining appropriate levels of BH4, which is vital for neuronal function and overall metabolic health. Dysregulation of GCHFR has been implicated in various neurological disorders, such as Parkinson’s disease, depression, and schizophrenia, where impaired neurotransmitter synthesis occurs. Recent studies have focused on the recombinant expression of GCHFR to better understand its structure-function relationships and regulatory mechanisms. By producing GCHFR as a recombinant protein, researchers aim to elucidate its catalytic properties and interactions with other molecules, allowing for a deeper insight into its role in both normal physiology and pathological conditions. This research not only contributes to basic biochemical knowledge but also holds potential therapeutic implications, as targeting GCHFR activity may provide novel strategies for modulating neurotransmitter levels in neuropsychiatric disorders. Additionally, understanding GCHFR’s mechanisms could pave the way for the development of small molecules or biologics that can enhance its activity or restore its function in pathological states. Overall, the study of GCHFR recombinant protein synthesis represents a promising avenue for advancing our understanding of neurotransmitter regulation and developing interventions for related diseases.
