Analytical Data
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Gene name
FDFT1
- Application
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Alternative Names
FDFT1;Squalene synthase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P37268
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Expression Region
1-283aa
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AA 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
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Molecular Weight
35 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
FDFT1, or Farnesyl Diphosphate Synthase 1, is an enzyme that plays a crucial role in the mevalonate pathway, which is essential for the biosynthesis of sterols and isoprenoids in eukaryotic cells. This pathway is vital for producing cholesterol, a fundamental component of cell membranes, and precursors for various signaling molecules. Dysregulation of FDFT1 has been linked to several diseases, including cancer, cardiovascular disorders, and neurodegenerative conditions, highlighting its potential as a therapeutic target. Research on the recombinant protein FDFT1 aims to better understand its enzymatic mechanisms, substrate specificity, and regulation, facilitating the development of inhibitors that could serve as clinical treatments. Recent advancements in structural biology and protein engineering techniques have enhanced our ability to produce and characterize FDFT1, allowing for detailed studies of its active site and interaction with regulatory molecules. The investigation of FDFT1 not only provides insights into fundamental metabolic processes but also offers a pathway for developing novel therapeutics aimed at modulating lipid metabolism and related diseases.
