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Recombinant Mouse FABP5/E-FABP Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Format
Carrier-Free

Order Details

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Recombinant Mouse FABP5/E-FABP Protein, CF Summary

Details of Functionality
Bioassay data are not available.
Source
E. coli-derived mouse FABP5/E-FABP protein
Met HHHHHH GS Mouse FABP5/E-FABP
(Met1-Gln135)
Accession # Q05816
N-terminus C-terminus
Accession #
N-terminal Sequence
Met
Protein/Peptide Type
Innovator Recombinant Proteins
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity not tested
Theoretical MW
16 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
16 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in NaPO4, NaCl and Tween®-20.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 400 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse FABP5/E-FABP Protein, CF

  • EFABP
  • E-FABP
  • E-FABPPAFABP
  • FABP5
  • fatty acid binding protein 5 (psoriasis-associated)
  • Fatty acid-binding protein 5
  • PA-FABPepidermal
  • Psoriasis-associated fatty acid-binding protein homolog

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 (1). 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 (2). 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 (3). 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 (1). 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 (4).

  1. Smathers, R. et al. (2011) Hum. Genomics. 5:170.
  2. Furuhashi, M. et al. (2008) Nat. Rev. Drug Discov. 7:489.
  3. Storch, J. et al. (2010) J. Biol. Chem. 285:32679.
  4. Bleck, B. et al. (1998) Gene 215:123.

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