A highly purified protein for fatty acid research
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FABP3 (human, recombinant)

Item No. 10007432

Technical Information
Synonyms
  • Fatty Acid Binding Protein 3
  • Heart-FABP
  • Heart-type Fatty Acid Binding Protein
  • H-FABP
  • Mammary-derived Growth Inhibitor
  • MDGI
  • M-FABP
  • Muscle Fatty Acid Binding Protein
Purity
≥95% estimated by SDS-PAGE
Source
Recombinant N-terminal His-tag protein expressed in E. coli
Amino Acids
1-133 (full length)
MW
19 kDa
50 mM of sodium phosphate, pH 7.2, with 150 mM sodium chloride and 20% glycerol
UniProt Accession №
P05413
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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Certificates of Analysis & Batch Specific Data

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    Product Description

    Fatty acid binding protein 3 (FABP3) is one of nine known cytosolic FABPs ranging in size from 14-15 kDa containing 127-132 amino acids.1 Members of this protein family exhibit high affinity for small lipophilic ligands and were named according to the tissue from which they were initially isolated.1 Studies suggest that FABPs are involved in the uptake and metabolism of fatty acids, in the maintenance of cellular membrane fatty acid levels, in intracellular trafficking of these substrates, in the modulation of specific enzymes of lipid metabolic pathways, and in the modulation of cell growth and differentiation.2 FABP family members have highly conserved three dimensional structures and 22-73% amino acid sequence similarity. FABP3 is composed of ten antiparallel β strands that form a barrel and is the most widely distributed FABP. It is found in heart, skeletal and smooth muscle, mammary epithelial cells, aorta, distal tubules of the kidney, lung, brain, placenta, and ovary. FABP3 is a potential biomarker for myocardial injury, especially for early detection of acute myocardial infarction (AMI).1

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Zimmerman, A.W., and Veerkamp, J.H. New insights into the structure and function of fatty acid-binding proteins. Cell. Mol. Life Sci. 59(7), 1096-1116 (2002).

    2. Massolini, G., and Calleri, E. Survey of binding properties of fatty acid-binding proteins chromatographic methods. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 797(1-2), 255-268 (2003).