Recombinant Human FABP1/L-FABP Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Format
Carrier-Free

Order Details

Recombinant Human FABP1/L-FABP Protein, CF Summary

Details of Functionality
Bioassay data are not available.
Source
E. coli-derived human FABP1/L-FABP protein
Ser2-Ile127, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Ser2
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

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
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 PBS, EDTA and DTT.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 1 mg/mL in PBS.

Notes

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

Alternate Names for Recombinant Human 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 protein-1 (FABP1; also named L- or liver FABP, hepatic FABP, Z protein, and heme-binding protein) is a member of a large superfamily of lipid binding proteins that are expressed in a tissue specific manner (1, 10, 11). FABP1 is one of ten cytoplasmic FABPs that are 14-15 kDa in size and range from 126‑140 amino acids (aa) in length (1, 2, 3). Although all are highly conserved in their tertiary structure, there is only modest aa identity between any two members. The FABP family members are subdivided based on organ or tissue type it was originally expressed or identified; liver- (L-FABP), intestine- (I-FABP), heart- (H-FABP), adipocyte- (A-FABP), epidermal- (E-FABP), ileal- (IL-FABP), brain- (B-FABP), myelin- (M-FABP) and testis-FABP (T-FABP) (1). Human L-FABP, the product of the FABP1 gene, is a 127 aa cytosolic protein that shows a flattened beta -barrel structure generated by a series of antiparallel beta -strands and two alpha ‑helices (4, 7). Unlike other members in the FABP family, each molecule of FABP1 is capable of binding two molecules of long-chain fatty acids. Other ligands may include heme, steroids, acyl CoAs, oxidized/peroxidized fatty acids, leukotrienes, prostaglandins and peroxisome proliferators (5, 6, 7, 13). It is suggested that ligands first bind to the outside of the molecule, and this binding subsequently induces a conformational change in the binding protein, resulting in "internalization" of the ligand (7, 12). An Ala-to-Thr polymorphism at position # 54 has been associated with an increased risk of type II diabetes (7, 10) and a Thr-to-Ala polymorphism at position # 94 has been reported to increase cholesterol binding affinity (8). Human FABP1 is 84%, 82% and 90% aa identical to mouse, rat and canine FABP1, respectively (9). It also shows 29% and 24% aa identity to human H-FABP and I‑FABP, respectively.
  1. Smathers, R & Petersen, D. (2011) Human Genomics 5:170.
  2. Storch, J. & Thumser, AE. (2000) Biochim Biophys Acta. 1486:28.
  3. Mihajlovic,M. & Lazaridis, T. (2007) Protein Sci. 9:2042.
  4. Sweetser, D.A. et al. (1987) J. Biol. Chem. 262:16060.
  5. Wang, G. et al. (2015) J Lipid Res. 56:2238.
  6. Thompson, J. et al. (1997) J. Biol. Chem. 272:7140.
  7. Bernlohr, DA. et al. (1997) Ann. Rev. of Nut. 17:277.
  8. Huang, H. et al. (2015) Biochim Biophys Acta. 1851:946
  9. Lowe J.B. et al. (1985) J. Biol. Chem. 260:3413.
  10. Zimmerman, A.W. and J.H. Veerkamp (2002) Cell. Mol. Life Sci. 59:1096.
  11. Haunerland, N.H. and F. Spener (2004) Prog. Lipid Res. 43:328.
  12. Majava,V. et al. (2010) PLoS One. 5:e10300.
  13. Veerkamp JH, Maatman RGHJ. (1995) Prog. Lipid Res. 34:17.

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