Abbreviation: FABP5
Target Synonym: Fatty acid-binding protein 5;Epidermal-type fatty acid-binding protein;E-FABP;Fatty acid-binding protein;epidermal;Keratinocyte lipid-binding protein;Psoriasis-associated fatty acid-binding protein homolog;PA-FABP
Target Species: Mouse
Expression Host: E.coli
Fusion Tag: N-His
UNIProt ID: Q05816
Background: Fatty acid binding proteins (FABP) are small cytoplasmic lipid binding proteins that are expressed in a tissue specific manner and are involved in intracellular lipid transport. All FABPs bind free fatty acids, cholesterol, and retinoids, which differ in their selectivity, affinity and binding mechanism. Circulating FABP levels are used as indicators of tissue damage. Some FABP polymorphisms have been associated with disorders of lipid metabolism and the development of atherosclerosis. FABPs are structurally conserved, consisting of a water-filled, ligand-binding pocket surrounded by ten anti-parallel beta-barrel structures, capped by an N-terminal helix-turn-helix motif. The helical N-terminus is involved in the regulation of FA transfer from membranes. FABP5, also known as epidermal fatty acid binding protein (E-FABP), is highly expressed in epidermal cells, but also in a plethora of other tissues, including mammary gland, brain, liver, kidney, lung, adipocytes, macrophages, tongue and testis. It is associated with keratinocytes and adipocytes and is suggested to promote fatty acid availability to enzymes, protect cell structures from fatty acid attack, and target fatty acids to nuclear transcription factors. The amino acid sequence of human FABP5 is 80%, 81% and 92% identical to that of mouse, rat and bovine FABP5, respectively.
Sequence: Ala 2-Gln 135
Purity: > 95 % as determined by reducing SDS-PAGE.
Formulation: Lyophilized from sterile PBS, pH 7.4.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Endotoxin: Please contact us for more information.
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