Analytical Data
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Gene name
FABP3
- Application
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P05413
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Expression Region
M1-A133
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Protein Length
Full Length
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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
Fatty Acid-Binding Protein 3 (FABP3), also known as heart-type FABP, is a pivotal protein that plays a critical role in the cellular uptake, transport, and metabolism of fatty acids within cardiac tissues. It is primarily expressed in the heart and skeletal muscles, where it facilitates the delivery of fatty acids to the mitochondria for beta-oxidation, thereby providing vital energy for myocardial contraction. Research on recombinant FABP3 has intensified due to its implications in various physiological and pathological conditions, including obesity, diabetes, and cardiovascular diseases. Understanding the structure and function of FABP3 can shed light on its role in lipid metabolism and energy homeostasis. Moreover, the recombinant production of FABP3 offers valuable opportunities for exploring its biophysical properties, protein interaction networks, and potential as a biomarker for heart-related diseases. By utilizing techniques such as recombinant DNA technology, researchers aim to generate and characterize extracellular and intracellular forms of FABP3, which can further aid in developing therapeutic strategies targeting lipid dysregulation in metabolic disorders. Insights gleaned from such studies could ultimately contribute to innovative treatments that mitigate the risk factors associated with heart disease and improve overall cardiac health. Thus, the exploration of recombinant FABP3 not only enhances our understanding of fundamental biochemical processes but also holds promise for translational applications in medicine.
