Cayman Chemical | FABP4 (human recombinant) • A-FABP; ALBP; Adipocyte-FABP; Fatty Acid Binding Protein 4; aP2; Adipocyte Fatty Acid Binding Protein

FABP4 (human recombinant)

Cayman Chemical Item Number 10009549

A-FABP; ALBP; Adipocyte-FABP; Fatty Acid Binding Protein 4; aP₂; Adipocyte Fatty Acid Binding Protein

Synonyms

A-FABP
ALBP
Adipocyte-FABP
Fatty Acid Binding Protein 4
aP2
Adipocyte Fatty Acid Binding Protein

Formulation

A solution in 50 mM of sodium phosphate, pH 7.2, containing 150 mM sodium chloride, and 20% glycerol

Purity

>90%

Stability

1 year

Storage

-80°C

Shipping

Dry Ice in continental US; may vary elsewhere

Description

Source: recombinant hexahistidine-tagged protein expressed in E. coli · M_r: ~18.8 kDa · Fatty acid binding protein-4 (FABP4; Adipocyte-FABP) is one of nine known cytosolic fatty acid binding proteins 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 Studies using FABP4 gene deletion in mice indicate a dominant role for FABP4 in several chronic metabolic diseases. Therefore, inhibiting the function of FABP4 is a potential mechanism for the treatment of metabolic diseases like diabetes and atherosclerosis.^3,4

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

2 Massolini, G., Calleri, E. Survey of binding properties of fatty acid-binding proteins chromatographic methods. J Chromatogr B 797 255-268 (2003).

3 Furuhashi, M., Tuncman, G., Görgün, C.Z., et al. Treatment of diabetes and atherosclerosis by inhibiting fatty-acid-binding protein aP₂. Nature 447 959-965 (2007).

4 Boord, J.B., Maeda, K., Makowski, L., et al. Adipocyte fatty acid-binding protein, aP₂, alters late atherosclerotic lesion formation in severe hypercholesterolemia. Arterioscler Thromb Vasc Biol 22 1686-1691 (2002).

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

Massolini, G., Calleri, E. Survey of binding properties of fatty acid-binding proteins chromatographic methods. J Chromatogr B 797 255-268 (2003).

Boord, J.B., Maeda, K., Makowski, L., et al. Adipocyte fatty acid-binding protein, aP₂, alters late atherosclerotic lesion formation in severe hypercholesterolemia. Arterioscler Thromb Vasc Biol 22 1686-1691 (2002).

Furuhashi, M., Tuncman, G., Görgün, C.Z., et al. Treatment of diabetes and atherosclerosis by inhibiting fatty-acid-binding protein aP₂. Nature 447 959-965 (2007).

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