Analytical Data
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Gene name
FPGS
- Application
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Alternative Names
Folylpoly-gamma-glutamate synthetase; Tetrahydrofolylpolyglutamate synthase; Tetrahydrofolate synthase
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Species
Mouse
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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
P48760
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Expression Region
Thr210~Cys439
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Molecular Weight
29kDa
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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
FPGS (folylpolyglutamate synthetase) is an enzyme that plays a crucial role in the metabolism of folate, a vitamin essential for DNA synthesis, repair, and methylation processes. The recombinant protein of FPGS has garnered significant research interest due to its potential applications in cancer therapy and metabolic disorders. In particular, the enzyme is involved in the polyglutamation of folate and its analogs, which enhances their retention in cells and improves their efficacy as chemotherapeutic agents. Understanding the structure and function of recombinant FPGS can lead to the development of novel folate-based drugs that target cancer cells more effectively while minimizing side effects. Furthermore, the study of FPGS provides insights into folate metabolism and its dysregulation in various diseases, including certain types of cancer and congenital disorders associated with folate deficiency. By exploring FPGS at the molecular level through recombinant protein technologies, researchers aim to unlock new therapeutic avenues that leverage the enzyme's unique properties, ultimately contributing to advancements in precision medicine and targeted therapies.
