Analytical Data
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Gene name
FDFT1
- Application
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Alternative Names
FPP:FPP farnesyltransferase Farnesyl-diphosphate farnesyltransferase
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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
P37268
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Expression Region
2-417aa
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Molecular Weight
52 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
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Protein Description
FDFT1, or Farnesyl-diphosphate farnesyltransferase 1, is an enzyme involved in the mevalonate pathway, which is crucial for the biosynthesis of sterols and isoprenoids in eukaryotic cells. Its primary function is to catalyze the transfer of farnesyl groups to proteins, a process known as protein farnesylation, which is essential for the proper localization, function, and stability of various signaling proteins, particularly in the Ras oncogene family. Mutations or dysregulation of FDFT1 can lead to numerous diseases, including various types of cancer and metabolic disorders. Recent studies have focused on the potential of FDFT1 as a therapeutic target, especially in cancer treatment, given its involvement in cell proliferation and survival pathways. Researchers are increasingly interested in characterizing the structure and function of recombinant FDFT1, utilizing techniques such as protein engineering and crystallography, to elucidate its mechanisms of action and interactions with other biomolecules. This knowledge may lead to the development of specific inhibitors that could provide novel therapeutic strategies for diseases linked to FDFT1. Furthermore, understanding the enzyme's role in lipid metabolism has broader implications in studying metabolic syndromes and cardiovascular diseases. As such, ongoing research into FDFT1 and its recombinant forms is critical for advancing our understanding of enzyme regulation, protein synthesis, and the development of targeted therapies.
