Recombinant Human FABP9/T-FABP Protein, CF Summary
Product Specifications
Met1-Val132, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
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.
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Reconstitution Calculator
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.
- Smathers, R & Petersen, D. (2011) Human Genomics 5:170.
- Storch, J. & Thumser, AE. (2000) Biochim Biophys Acta. 1486:28.
- Zimmerman, A.W. & Veerkamp, J.H. (2007) Protein Sci. 9:2042.
- Bernlohr, D. et al. (1997) Ann. Rev. of Nut. 17:277.
- Majava,V. et al. (2010) PLoS One. 5:e10300.
- Zimmerman, A.W. and J.H. Veerkamp (2002) Cell. Mol. Life Sci. 59:1096.
- Haunerland, N.H. and F. Spener (2004) Prog. Lipid Res. 43:328.
- Oko, R. & Morales, C.R. (1994) Dev Biol. 166:235.
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