Analytical Data
-
Gene name
FDPS
- Application
-
Alternative Names
(2E,6E)-farnesyl diphosphate synthase Dimethylallyltranstransferase (EC:2.5.1.1) Farnesyl diphosphate synthase Geranyltranstransferase
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P14324
-
Expression Region
1-419aa
-
Molecular Weight
64.3 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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 a key enzyme involved in the mevalonate pathway, which is crucial for the biosynthesis of isoprenoids, including cholesterol and other essential biomolecules. Research on FDPS has garnered significant attention due to its role in various biological processes and diseases, including cancer and cardiovascular disorders. The enzyme catalyzes the condensation of isopentenyl diphosphate with dimethylallyl diphosphate to produce farnesyl diphosphate, a vital precursor for the synthesis of lipid-modified proteins. Dysregulation of FDPS activity has been implicated in oncogenic signaling pathways, making it a potential target for therapeutic interventions. Furthermore, studies have demonstrated that FDPS can be influenced by various inhibitors, leading to a growing interest in the development of FDPS-targeted drugs. In recent years, advances in recombinant DNA technology and protein expression systems have enabled researchers to produce and characterize FDPS proteins in vitro, facilitating detailed kinetic studies and structure-function analyses. Understanding the molecular mechanisms of FDPS and its interactions with inhibitors may provide insights into new treatment strategies for diseases associated with abnormal isoprenoid metabolism. Thus, ongoing research into FDPS recombinant proteins is essential for elucidating their biological significance and exploring their potential as drug targets in the context of disease management.
