Analytical Data
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Gene name
FABP2
- Application
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Alternative Names
Fatty acid-binding protein 2;Intestinal-type fatty acid-binding protein;I-FABP
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Species
Human
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Source
E. coli
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Tag
N-terminal His Tag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P12104
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Expression Region
1-132aa
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AA Sequence
MAFDSTWKVDRSENYDKFMEKMGVNIVKRKLAAHDNLKLTITQEGNKFTVKESS TFRNIEVVFELGVTFNYNLADGTELRGTWSLEGNKLIGKFKRTDNGNELNTVRE IIGDELVQTYVYEGVEAKRIFKKD
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Protein Length
Full Length
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Molecular Weight
18.9kDa
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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
Identification
Protein Description
Fatty acid-binding protein 2 (FABP2), also known as intestinal-FABP (I-FABP), is a protein predominantly expressed in enterocytes of the small intestine, playing a crucial role in lipid metabolism and transport. The significance of FABP2/I-FABP has gained attention in recent years due to its involvement in various physiological and pathological processes, including obesity, diabetes, and metabolic syndrome. Abnormal levels of I-FABP have been associated with increased intestinal permeability and inflammation, providing insights into the pathophysiology of gastrointestinal disorders. Research on recombinant FABP2/I-FABP has been propelled by the need for better understanding of its structure-function relationships and potential therapeutic applications. Recombinant protein forms of FABP2/I-FABP allow for detailed biochemical studies and offer opportunities for developing diagnostic markers or innovative treatments targeting metabolic diseases. The expression, purification, and characterization of recombinant FABP2/I-FABP contribute to elucidating its mechanism of action, binding properties, and interactions with fatty acids and other molecules. Furthermore, the study of recombinant I-FABP can facilitate the exploration of its potential as a biomarker for intestinal injury and functionality, paving the way for novel therapeutic strategies aimed at metabolic dysregulation and related inflammatory conditions. Overall, the exploration of recombinant FABP2/I-FABP represents a promising frontier in understanding lipid metabolism and developing interventions for metabolic disorders.
