Analytical Data
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Gene name
FAS
- Application
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Alternative Names
FAS；FAS；Fatty acid 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
P25445
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Expression Region
1-235aa
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AA Sequence
MLGIWTLLPLVLTSVARLSSKSVNAQVTDINSKGLELRKTVTTVETQNLE GLHHDGQFCHKPCPPGERKARDCTVNGDEPDCVPCQEGKEYTDKAHFSSK CRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNSTVCEHCDPCTKCE HGIIKECTLTSNTKCKEEGSRSNLGWLCLLLLPIPLIVWVKRKEVQKTCR KHRKENQGSHESPTLNPETVAINLSDVDLSKYITTIAGVMTLSQVKGFVR KNGVNEAKIDEIKNDNVQDTAEQKVQLLRNWHQLHGKKEAYDTLIKDLKK ANLCTLAEKIQTIILKDITSDSENSNFRNEIQSLV
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Molecular Weight
62 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
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Protein Description
FAS (Fatty Acid Synthase) is a critical enzyme complex involved in the de novo synthesis of fatty acids, playing a pivotal role in lipid metabolism and energy homeostasis. Its dysregulation has been linked to various metabolic disorders, including obesity, diabetes, and cancer, making FAS a significant target for therapeutic intervention. The study of FAS recombinant proteins has gained traction due to their potential applications in drug development and metabolic research. By expressing FAS in a recombinant system, researchers can obtain large quantities of the enzyme, enabling detailed studies of its structure, function, and interaction with other biomolecules. These recombinant proteins serve as valuable tools for elucidating the molecular mechanisms underlying fatty acid metabolism, providing insights into how aberrations in these pathways contribute to disease. Furthermore, the characterization of FAS inhibitors can lead to novel strategies for treating metabolic diseases. In recent years, advancements in protein engineering and expression systems have facilitated the production and purification of FAS recombinant proteins, allowing for high-throughput screening of potential inhibitors and enhancing our understanding of FAS regulation. This robust research background sets the stage for ongoing investigations into the role of FAS in health and disease, highlighting its significance in metabolic regulation and the development of targeted therapies.
