Analytical Data
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Gene name
FDPS
- Application
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Alternative Names
FDPS；FPS；KIAA1293；Farnesyl pyrophosphate synthase
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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
P14324
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Expression Region
1-419aa
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AA Sequence
MPLSRWLRSVGVFLLPAPYWAPRERWLGSLRRPSLVHGYPVLAWHSARCWCQAWTEEPRALCSSLRMNGDQNSDVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGKYNRGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKRRK
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Molecular Weight
64.3kDa
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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
FDPS (Farnesyl Diphosphate Synthase) is an essential enzyme involved in the mevalonate pathway, which is critical for the biosynthesis of isoprenoids, including sterols and other vital biomolecules. The study of FDPS recombinant proteins has gained significant interest due to their role in various biological processes and their potential implications in diseases such as cancer, cardiovascular disorders, and metabolic syndromes. This enzyme catalyzes the formation of farnesyl diphosphate from isopentenyl diphosphate and dimethylallyl diphosphate, a pivotal step in the synthesis of lipids and prenylated proteins. The understanding of FDPS function and regulation is essential in drug discovery, particularly for developing inhibitors that could serve as therapeutic agents against cancer, as cancer cells often exhibit dysregulated lipid metabolism. Recombinant protein technology has facilitated the production of FDPS in various expression systems, allowing researchers to investigate its structure, enzyme kinetics, and interactions with potential inhibitors. Furthermore, the study of FDPS has broader implications in comprehending the metabolic pathways that sustain cell proliferation and survival. As scientists explore the complexities of FDPS and its role within the mevalonate pathway, there is a growing potential for developing novel therapeutic strategies targeting this enzyme, highlighting the importance of its research in health and disease.
