protein

FDFT1 Protein, Human (His)

HY-P72193

20 μg;50 μg

158;300 USD

FDFT1 Protein, Human (His)

proteins

E. coli

20 μg;50 μg

158;300 USD

FDFT1 is a key enzyme in cellular metabolism responsible for coordinating the condensation of two farnesyl pyrophosphate (FPP) molecules, a key step in sterol biosynthesis. The process proceeds in two distinct steps: First, two FPP molecules react to form the stable squalene diphosphate intermediate (PSQPP), releasing protons and inorganic diphosphate. FDFT1 Protein, Human (His) is the recombinant human-derived FDFT1 protein, expressed by E. coli , with N-6*His labeled tag.

Human

FDFT1, or squalene synthase, is a crucial enzyme that plays a pivotal role in sterol biosynthesis. Functioning as the first committed enzyme in this pathway, FDFT1 catalyzes the condensation of two farnesyl pyrophosphate (FPP) molecules to form squalene through a two-step process. In the initial half-reaction, two FPP molecules react to generate the stable presqualene diphosphate intermediate (PSQPP), accompanied by the release of a proton and inorganic diphosphate. Subsequently, in the second half-reaction, PSQPP undergoes heterolysis, isomerization, and reduction with either NADPH or NADH, ultimately producing squalene. This enzymatic process is fundamental for the synthesis of sterols, highlighting the central role of FDFT1 in governing the initial steps of sterol biosynthesis.

DGPT; ERG9; Farnesyl diphosphate farnesyltransferase; Farnesyl-diphosphate farnesyltransferase; FDFT_HUMAN; FDFT1; FPP:FPP farnesyltransferase; SQS; Squalene synthase; Squalene synthetase; SS

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm solution of 10 mM Tris-HCl, 1 mM EDTA, 6% Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.