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
Related Products
Protein Description
The study of FAS (Fatty Acid Synthase) recombinant proteins has garnered significant attention in recent years due to the central role of FAS in lipid metabolism and its implications in various diseases, particularly cancer and metabolic disorders. FAS is an essential multi-enzyme complex responsible for the de novo synthesis of fatty acids, which are crucial for cellular membrane composition, energy storage, and signaling pathways. Overexpression of FAS is commonly observed in many cancers, making it a potential biomarker and therapeutic target. Researchers have been developing recombinant forms of FAS to better understand its structure-function relationships and to explore its enzymatic mechanisms. The use of recombinant protein techniques has enabled scientists to produce purified FAS enzymes, allowing for detailed biochemical analyses, and the potential development of FAS inhibitors as anti-cancer agents. The manipulation of FAS through recombinant technology also opens avenues for metabolic engineering, providing insights into lipid-related metabolic pathways. Overall, the exploration of FAS recombinant proteins is pivotal in advancing therapeutic strategies against diseases linked to lipid metabolism and in understanding the biological functions of fatty acids within the cell.
