Recombinant Rat FABP1/L-FABP Protein, CF

• Reactivity: Rt
• Format: Carrier-Free

Recombinant Rat FABP1/L-FABP Protein, CF Summary

• Details of Functionality: Bioassay data are not available.
• Source: E. coli-derived rat FABP1/L-FABP protein
  

  Met	HHHHHH	GS	Rat FABP1/L-FABP (Met1-Ile127) Accession # P02692
  N-terminus			C-terminus

• Accession #: P02692
• 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: 15 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: 14 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage:
  • 6 months from date of receipt, 2 to 8 °C as supplied.
  • 3 months, 2 to 8 °C under sterile conditions after opening.
• Buffer: Supplied as a 0.2 μm filtered solution in PBS, DTT and Glycerol.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Notes

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

Alternate Names for Recombinant Rat FABP1/L-FABP Protein, CF

• FABP1
• FABPL
• fatty acid binding protein 1, liver
• fatty acid-binding protein, liver
• LFABP
• L-FABP
• L-FABPFatty acid-binding protein 1
• Liver-type fatty acid-binding protein

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). FABP1, also known as liver FABP (L-FABP) is highly expressed in the liver, intestine, kidney and lung (1). FABP1 binds free fatty acids and their co-enzyme A derivatives. FABP1 is unique among other members in FABP family, attributed to its ability to bind multiple ligands at once. It has a larger solvent-accessible core in comparison to other FABPs, and this allows for more diverse binding to substrates (1). Rat FABP1 is 127 amino acids (aa) in length. It is a two beta-sheet molecule that contains an acetylated initiating methionine. Full-length mouse FABP1 shares 94% and 82% aa identity with rat and human FABP1, respectively (4).

1. Smathers, R. et al. (2011) Hum. Genomics. 5(3):170.
2. Furuhashi, M. et al. (2008) Nat. Rev. Drug Discov. 7(6):489.
3. Storch, J. et al. (2010) J. Biol. Chem. 285(43):32679.
4. Sweetser, D., et al. (1987) J. Biol. Chem. 262(33):16060.

Bioinformatics

• Uniprot:
  • P02692()