Analytical Data
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Gene name
FATP1
- Application
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Alternative Names
SLC27A1; ACSVL5; FATP; Long-Chain Fatty Acid Transport Protein 1; Solute Carrier Family 27 Member 1,Fatty Acid Transporter
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P97849
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Expression Region
Glu191~Lys475
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Molecular Weight
35kDa
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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
FATP1 (Fatty Acid Transporter Protein 1) is a crucial membrane protein involved in the uptake and transportation of long-chain fatty acids within cells, playing a vital role in lipid metabolism and energy homeostasis. Its dysfunction is linked to various metabolic disorders, including obesity, type 2 diabetes, and cardiovascular diseases, making it an important target for biomedical research. Recent studies have highlighted the significance of FATP1 in regulating intracellular fatty acid levels and its involvement in the inflammatory response in adipose tissues. With the rise of metabolic diseases globally, understanding FATP1's function and regulation is paramount for developing potential therapeutic interventions. The recombinant expression of FATP1 enables researchers to create purified protein for detailed biochemical and structural studies, which are essential for elucidating its transport mechanisms and interactions with fatty acids. Moreover, exploring FATP1's potential as a therapeutic target through small-molecule inhibitors or modulators holds promise in combating metabolic-related diseases. Thus, ongoing research on FATP1 not only enhances our understanding of lipid metabolism but also paves the way for novel approaches to treat metabolic disorders.
