Recombinant Human FABP8/M-FABP Protein, CF

• Reactivity: Hu
• Format: Carrier-Free

Recombinant Human FABP8/M-FABP Protein, CF Summary

• Details of Functionality: Bioassay data are not available.
• Source: E. coli-derived human FABP8/M-FABP protein
  Ser2-Val132, with a C-terminal 6-His tag
• Accession #: P02689
• 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

• 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 conditons

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 Sodium Acetate.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Reconstitution Instructions: Reconstitute at 1 mg/mL in water.

Notes

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

Alternate Names for Recombinant Human FABP8/M-FABP Protein, CF

• FABP8
• MFABP
• M-FABP
• MP2
• myelin P2 protein
• P2
• peripheral myelin protein 2FABP8
• PMP2

Background

Fatty acid binding protein-8 (FABP8; also named Peripheral myelin protein 2, M- (myelin) FABP, Myelin P2 Protein, MP2, or P2) is a member of a large superfamily of lipid binding proteins that are expressed in a tissue specific manner (1, 8, 9). FABP-8 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 M-FABP, the product of the PMP2 gene, is a 131 aa cytosolic protein that shows a flattened beta -barrel structure generated by a series of antiparallel beta -strands and two alpha ‑helices (4, 7, 10). One molecule of FABP-8 is capable of binding one long-chain fatty acid (1, 5, 6). 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 (5, 6, 7). Human FABP-8 is 87%, 92% and 83% aa identical to mouse, bovine and horse FABP-8, respectively. It also shows 26% and 30% aa identity to human L-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. Zimmerman, A.W. & Veerkamp, J.H. (2007) Protein Sci. 9:2042.
4. Jones, TA. (1988) The EMBO Journal. 7:1 597.
5. Majava,V. et al. (2010) PLoS One. 5:e10300.
6. Ruskamo, S. et al. (2014) Acta Crystallogr D Biol Crystallogr. 70:165.
7. Bernlohr, D. et al. (1997) Ann. Rev. of Nut. 17:277.
8. Zimmerman, A.W. and J.H. Veerkamp (2002) Cell. Mol. Life Sci. 59:1096.
9. Haunerland, N.H. and F. Spener (2004) Prog. Lipid Res. 43:328.
10. Suzuki, M. et al. (1982) J Neurochem. 39:1759.

Bioinformatics

• Uniprot:
  • P02689(Human)