protein

FDPS Protein, Human (His)

HY-P75197

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

74;125;350;595;1480;2220 USD

FDPS Protein, Human (His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

74;125;350;595;1480;2220 USD

FDPS Protein, a key enzyme in isoprenoid biosynthesis, catalyzes the formation of farnesyl diphosphate (FPP). FPP is a precursor for essential metabolites like sterols, dolichols, carotenoids, and ubiquinones. It also serves as a substrate for protein farnesylation and geranylgeranylation. FDPS sequentially condenses isopentenyl pyrophosphate with dimethylallyl pyrophosphate and then with geranylpyrophosphate to produce farnesyl pyrophosphate. FDPS Protein, Human (His) is the recombinant human-derived FDPS protein, expressed by E. coli , with N-His labeled tag. The total length of FDPS Protein, Human (His) is 353 a.a., with molecular weight of ~41 kDa.

Human

FDPS protein plays a pivotal role in isoprenoid biosynthesis, serving as the key enzyme that orchestrates the sequential condensation of isopentenyl pyrophosphate with allylic pyrophosphates. This enzymatic process includes the successive combination with dimethylallyl pyrophosphate, leading to the formation of geranylpyrophosphate and culminating in the generation of farnesyl diphosphate (FPP). Notably, FPP acts as a critical precursor for the biosynthesis of various essential metabolites, such as sterols, dolichols, carotenoids, and ubiquinones. Additionally, FPP serves as a substrate for protein farnesylation and geranylgeranylation, essential post-translational modifications that play crucial roles in cellular processes. The catalytic activity of FDPS underscores its significance in the synthesis of key molecules with diverse biological functions.

Farnesyl pyrophosphate synthase; FPP synthase; FPS; KIAA1293

Greater than 95% as determined by Tris-Bis PAGE.

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

Room temperature in continental US; may vary elsewhere.