Analytical Data
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Gene name
CTPS1
- Application
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Alternative Names
CTP synthetase 1 UTP--ammonia ligase 1
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Species
Human
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Source
Yeast
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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
P17812
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Expression Region
1-591aa
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Molecular Weight
68.7 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
CTPS1, or Cytidine Triphosphate Synthase 1, is a pivotal enzyme involved in the de novo synthesis of cytidine triphosphate (CTP), which is essential for the production of RNA and certain lipid molecules. Research into CTPS1 is particularly significant due to its critical role in cellular metabolism and proliferation, as well as its implications in various diseases, including cancer and viral infections. Abnormalities in CTP synthesis can disrupt normal cell functions, contributing to pathological conditions. The enzyme operates in a tightly regulated manner, influencing nucleotide pool balance, which is crucial for DNA and RNA synthesis. Recent studies have highlighted the therapeutic potential of targeting CTPS1 in cancer treatment, as inhibitors of this enzyme could selectively impair the proliferation of rapidly dividing cells. Additionally, understanding the structural and functional aspects of CTPS1 through recombinant protein studies has provided insights into its catalytic mechanisms and regulatory pathways, paving the way for developing novel inhibitors. This research not only enhances our comprehension of nucleotide metabolism but also holds promise for devising innovative strategies in drug development.
