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Amino acids 2-417 constitute the expression domain of recombinant Human FDFT1. This FDFT1 protein is theoretically predicted to have a molecular weight of 52 kDa. This FDFT1 protein is produced using e.coli expression system. The FDFT1 gene fragment has been modified by fusing the N-terminal 6xHis tag, providing convenience in detecting and purifying the recombinant FDFT1 protein during the following stages.Human squalene synthase (FDFT1) is a key enzyme in the cholesterol biosynthesis pathway, catalyzing the condensation of two molecules of farnesyl diphosphate to produce squalene. This reaction is a crucial step in the mevalonate pathway, leading to the synthesis of cholesterol and other isoprenoids. FDFT1 plays a central role in maintaining cellular lipid homeostasis. Dysregulation of cholesterol levels can contribute to various diseases, including cardiovascular disorders. Research on FDFT1 is important for understanding cholesterol metabolism and lipid-related diseases and exploring potential therapeutic targets for conditions associated with abnormal lipid profiles.
Amino acids 2-417 constitute the expression domain of recombinant Human FDFT1. This FDFT1 protein is theoretically predicted to have a molecular weight of 52 kDa. This FDFT1 protein is produced using e.coli expression system. The FDFT1 gene fragment has been modified by fusing the N-terminal 6xHis tag, providing convenience in detecting and purifying the recombinant FDFT1 protein during the following stages.Human squalene synthase (FDFT1) is a key enzyme in the cholesterol biosynthesis pathway, catalyzing the condensation of two molecules of farnesyl diphosphate to produce squalene. This reaction is a crucial step in the mevalonate pathway, leading to the synthesis of cholesterol and other isoprenoids. FDFT1 plays a central role in maintaining cellular lipid homeostasis. Dysregulation of cholesterol levels can contribute to various diseases, including cardiovascular disorders. Research on FDFT1 is important for understanding cholesterol metabolism and lipid-related diseases and exploring potential therapeutic targets for conditions associated with abnormal lipid profiles.
| Cat.No | ACP03725 | Target Name | FDFT1 |
|---|---|---|---|
| Target Synonyms | DGPT; ERG9; Farnesyl diphosphate farnesyltransferase; Farnesyl-diphosphate farnesyltransferase; FDFT_HUMAN; FDFT1; FPP:FPP farnesyltransferase; SQS; Squalene synthase; Squalene synthetase; SS | Form | Liquid or Lyophilized powder |
| Expression System | E.coli | Expression Range | 2-417aa |
| Mol Weight | 52.0kDa | Protein Length | Partial |
| Purity | Greater than 90% as determined by SDS-PAGE. | Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P37268 |
|---|
Uniprot Id
P37268
Target Species
Human
Target Name
FDFT1
Target Full Name
Squalene synthase
Target Function
Catalyzes the condensation of 2 farnesyl pyrophosphate (FPP) moieties to form squalene. Proceeds in two distinct steps. In the first half-reaction, two molecules of FPP react to form the stable presqualene diphosphate intermediate (PSQPP), with concomitant release of a proton and a molecule of inorganic diphosphate. In the second half-reaction, PSQPP undergoes heterolysis, isomerization, and reduction with NADPH or NADH to form squalene. It is the first committed enzyme of the sterol biosynthesis pathway.
Target Subcellular Location
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Target Protein Families
Phytoene/squalene synthase family
Target Tissue Specificity
Widely expressed.
Target Research Area
Metabolism
Target Synonyms
DGPT; ERG9; Farnesyl diphosphate farnesyltransferase; Farnesyl-diphosphate farnesyltransferase; FDFT_HUMAN; FDFT1; FPP:FPP farnesyltransferase; SQS; Squalene synthase; Squalene synthetase; SS
Target Background
This gene encodes a membrane-associated enzyme located at a branch point in the mevalonate pathway. The encoded protein is the first specific enzyme in cholesterol biosynthesis, catalyzing the dimerization of two molecules of farnesyl diphosphate in a two-step reaction to form squalene.
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