Analytical Data
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Gene name
FABP1/L-FABP
- Application
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Alternative Names
FABP-1; FABPL; L-FABP; LFABP; Liver-type fatty acid-binding protein; Fatty Acid Binding Protein 1, Liver
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P07148
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Expression Region
Ser2~Ile127
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Molecular Weight
13kDa
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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
Fatty acid binding protein 1 (FABP1), also known as liver-type fatty acid binding protein (L-FABP), plays a crucial role in lipid metabolism and homeostasis. It is predominantly expressed in the liver, where it functions to transport long-chain fatty acids and facilitate their uptake and metabolism within hepatocytes. The interest in FABP1/L-FABP has surged due to its involvement in various metabolic disorders, including obesity, diabetes, and non-alcoholic fatty liver disease (NAFLD). Studies have shown that alterations in FABP1 expression can significantly impact lipid droplet formation and fatty acid oxidation, linking it to the broader context of metabolic syndrome. Furthermore, FABP1's potential as a biomarker for liver diseases has also attracted attention. Researchers have been investigating the recombinant production of FABP1/L-FABP to better understand its structure-function relationship and to explore its therapeutic potential. By utilizing recombinant DNA technology, scientists can produce large quantities of pure FABP1 for detailed biochemical and biophysical studies, paving the way for insights into its mechanisms of action and potential as a drug target. The continued exploration of FABP1/L-FABP holds promise for developing strategies to manage and treat metabolic disorders, making it a valuable focus of biomedical research.
