FDFT1 Human

Farnesyl-Diphosphate Farnesyltransferase 1 Human Recombinant
Cat. No.
BT3904
Source
Escherichia Coli.
Synonyms
Farnesyl-Diphosphate Farnesyltransferase 1, Squalene Synthase, SQS, SS, FPP:FPP Farnesyltransferase, EC 2.5.1.21, DGPT, ERG9, Presqualene-Di-Diphosphate Synthase, Squalene Synthetase, Farnesyl-Diphosphate, Farnesyltransferase, FDFT1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

FDFT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 306 amino acids (1-283 a.a) and having a molecular mass of 35.4 kDa. 
FDFT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Farnesyl-Diphosphate Farnesyltransferase 1, also known as FDFT1, is a membrane-associated enzyme found at a branch point in the mevalonate pathway. FDFT1 is a member of the phytoene/squalene synthase family and acts as the first specific enzyme in cholesterol biosynthesis. It catalyzes a two-step reaction where two molecules of farnesyl diphosphate are dimerized to form squalene.
Description
Recombinant human FDFT1 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 306 amino acids (with amino acids 1-283 being the primary sequence) and has a molecular weight of 35.4 kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
Sterile, colorless solution.
Formulation
The FDFT1 protein solution is provided at a concentration of 0.25 mg/ml and contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, and 0.4M Urea.
Stability
For short-term storage (up to 2-4 weeks), keep the protein at 4°C. For long-term storage, freeze the protein at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 85.0% by SDS-PAGE analysis.
Synonyms
Farnesyl-Diphosphate Farnesyltransferase 1, Squalene Synthase, SQS, SS, FPP:FPP Farnesyltransferase, EC 2.5.1.21, DGPT, ERG9, Presqualene-Di-Diphosphate Synthase, Squalene Synthetase, Farnesyl-Diphosphate, Farnesyltransferase, FDFT1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEFVKCL GHPEEFYNLV RFRIGGKRKV MPKMDQDSLS SSLKTCYKYL NQTSRSFAAV IQALDGEMRN AVCIFYLVLR ALDTLEDDMT ISVEKKVPLL HNFHSFLYQP DWRFMESKEK DRQVLEDFPT ISLEFRNLAE KYQTVIADIC RRMGIGMAEF LDKHVTSEQE WDKYCHYVAG LVGIGLSRLF SASEFEDPLV GEDTERANSM GLFLQKTNII RDYLEDQQGG REFWPQEVWS RYVKKLGDFA KPENIDLAVQ CLNELITNAL HHIPDVITYL SRLRNQ.

Product Science Overview

Introduction

Farnesyl-Diphosphate Farnesyltransferase 1 (FDFT1), also known as squalene synthase, is a crucial enzyme in the biosynthesis of cholesterol. This enzyme is encoded by the FDFT1 gene in humans and plays a significant role in the mevalonate pathway, which is essential for the production of sterols, including cholesterol .

Structure and Function

FDFT1 is a membrane-associated enzyme that catalyzes the first committed step in cholesterol biosynthesis. It facilitates the dimerization of two molecules of farnesyl diphosphate (FPP) to form squalene in a two-step reaction . This reaction is pivotal as it marks the transition from the production of simple isoprenoids to the complex sterols.

Role in Cholesterol Biosynthesis

The mevalonate pathway, where FDFT1 operates, is a critical metabolic pathway that leads to the synthesis of cholesterol and other isoprenoids. Cholesterol is an essential biomolecule involved in various cellular processes, including membrane structure, hormone production, and signaling . The activity of FDFT1 is tightly regulated to maintain cholesterol homeostasis in the body.

Clinical Significance

FDFT1 has garnered attention for its role in various diseases, particularly those related to cholesterol metabolism. Abnormalities in cholesterol levels are linked to conditions such as hyperlipidemia, atherosclerosis, and certain types of cancer . Elevated expression of FDFT1 has been observed in some cancers, suggesting its potential as a biomarker for diagnosis and a target for therapeutic intervention .

Research and Therapeutic Potential

Recent studies have highlighted the importance of FDFT1 in cancer biology. The enzyme’s role in metabolic reprogramming, cell proliferation, and invasion makes it a promising target for cancer treatment . Inhibitors of FDFT1 are being explored not only to lower cholesterol levels but also as potential anticancer agents .

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