Recombinant Human FABP9/T-FABP Protein, CF

R&D Systems | Catalog # 9488-CL

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Key Product Details

  • R&D Systems E. coli-derived Recombinant Human FABP9/T-FABP Protein (9488-CL)
  • Quality control testing to verify active proteins with lot specific assays by in-house scientists
  • All R&D Systems proteins are covered with a 100% guarantee

Source

E. coli

Accession Number

Q0Z7S8
View all FABP9/T-FABP Proteins and Enzymes »

Product Specifications

Source

E. coli-derived human FABP9/T-FABP protein
Met1-Val132, with a C-terminal 6-His tag

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Met1

Predicted Molecular Mass

16 kDa

SDS-PAGE

15 kDa, reducing conditions

Activity

Bioassay data are not available.

Formulation, Preparation, and Storage

9488-CL
Formulation Lyophilized from a 0.2 μm filtered solution in PBS, EDTA and DTT.
Reconstitution

Reconstitute at 1 mg/mL in PBS.

Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: FABP9/T-FABP

Fatty acid binding protein-9 (FABP9; also named Testis lipid-binding protein, Testis-type fatty acid-binding protein, TLBP, T- FABP, PERF, or PERF15) is a member of a large superfamily of lipid binding proteins that are expressed in a tissue specific manner (1, 6, 7). FABP9 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 T‑FABP, the product of the FABP9 gene, is a 132 aa cytosolic protein that shows a flattened beta -barrel structure generated by a series of antiparallel beta -strands and two alpha ‑helices (4, 8). One molecule of FABP-9 is capable of binding one long-chain fatty acid (1, 5). 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 (4, 5). Human FABP-9 is 71%, 68% and 62% aa identical to mouse, rat and canine FABP-9, respectively. It also shows 26% and 28% aa identity to human L-FABP and I‑FABP, respectively.

References

  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. Bernlohr, D. et al. (1997) Ann. Rev. of Nut. 17:277.
  5. Majava,V. et al. (2010) PLoS One. 5:e10300.
  6. Zimmerman, A.W. and J.H. Veerkamp (2002) Cell. Mol. Life Sci. 59:1096.
  7. Haunerland, N.H. and F. Spener (2004) Prog. Lipid Res. 43:328.
  8. Oko, R. & Morales, C.R. (1994) Dev Biol. 166:235.

Long Name

Fatty Acid-Binding Protein 9

Alternate Names

PERF 15, T-FABP, TFABP

Entrez Gene IDs

646480 (Human); 21884 (Mouse)

Gene Symbol

FABP9

UniProt

Q0Z7S8

Additional FABP9/T-FABP Products

Product Documents for Recombinant Human FABP9/T-FABP Protein, CF

Certificate of Analysis

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Product Specific Notices for Recombinant Human FABP9/T-FABP Protein, CF

For research use only

Related Research Areas

Obesity
Primordial and Mature Germ Cells

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