Thermo Scientific Pierce Trifluoroacetic Acid (TFA) is manufactured and tested to meet strict specifications that ensure superior performance for use as an ion-pairing agent in reverse-phase peptide separations.
Trifluoroacetic acid (TFA) is the most commonly used ion pairing agent for use in reverse-phase HPLC peptide separations because it sharpens peaks and improves resolution, is volatile and easily removed, has low absorption within detection wavelengths, and has a proven history of use.
Highlights:
- High purity and exceptional clarity – allows sensitive, nondestructive peptide detection at low UV wavelengths in reverse-phase HPLC protein and peptide separation systems
- High-performance packaging – TFA packaged under nitrogen in amber glass ampules or bottles with protective PTFE-lined fluorocarbon caps to ensure TFA integrity
- Economical convenience – Choose the TFA format that works best for your application. In just a few seconds, 1 ml ampules can be used to prepare 1 liter of fresh 0.1% v/v trifluoroacetic acid solution for the mobile phase in reverse-phase chromatography
Applications:
- Ion pair reagent for reverse-phase HPLC
- Protein/peptide sequencing
- Protein/peptide solubilizing agent
- Solid-phase peptide synthesis
- Amino acid analysis
- Making 0.1% solutions of trifluoroacetic acid (w/v vs. v/v)
Product Details:
| General properties of trifluoroacetic acid |
| Alternative names |
Perfluoroacetic acid,
Trifluoroethanoic acid,
Trifluoracetic acid |
| Molecular formula |
CF3COOH |
| Molecular weight |
114.02 |
| Density |
1.53g/mL, 20°C |
| Melting / boiling point |
-15°C / 72°C |
| CAS number |
76-05-01 |
Thermo Scientific Pierce TFA is manufactured to the highest specifications to ensure the integrity of your data, maximize sensitivity in your assay and to prolong the life of your equipment.
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Specifications of Thermo Scientific Pierce TFA
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- TFA Purity: >=99.5%
- Water content: <=0.1%
- Chain length: <=99.5% C2
- Ninhydrin positives: A570 <=0.02 above blank
- Tollen’s test (aldehydes): Negative
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- UV Absorbance (0.1% aqueous)
- A280 <=0.002
- A254 <=0.005
- A230 <=0.090
- UV Absorbance (neat)
- A300 <=0.03
- A275 <=0.04
- Cut-off <=262nm
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Making 0.1% Trifluoracetic Acid Solutions:
For complex peptide separations, the key to success can be to vary selectivity. Varying mobile phase composition on the same column can change selectivity enough to resolve peptides that would otherwise overlap. Trifluoroacetic acid is the most frequently used modifier for peptide separations in reverse-phase HPLC. The TFA concentration usually specified is 0.1%. For reproducible separations from run-to-run or from lab-to-lab, it is essential to make TFA concentrations the same.
Trifluoroacetic acid concentration can and should be specified as either "w/v” (weight/volume), or as "v/v" (volume/volume). The w/v specification designates that the TFA is to be weighed and added to a volume of mobile phase (e.g. 0.1% TFA w/v requires one gram of TFA per liter). The v/v specification designates that the TFA is to be measured by volume (e.g. 0.1% TFA v/v requires one ml of TFA per liter).
Because the density of trifluoroacetic acid is 1.53 g/ml the difference between 0.1% TFA (w/v) and 0.1% TFA (v/v) is more than 50%. For the sake of reproducibility, it is essential for authors of a method to specify, and for users of a method to know, whether the TFA concentration is given as "w/v" or "v/v".
References:
- Che F.-Y. et al. (2011) Comprehensive proteomic analysis of membrane proteins in toxoplasma gondii. Mol. Cell. Proteomics. 10, M110.000745-.
- Agnes J. T. et al. (2011) Identification of anaplasma marginale outer membrane protein antigens conserved between a. Marginale sensu stricto strains and the live a. Marginale subsp. Centrale vaccine. Infect. Immun. 79, 1311-8.
- Warner A. H. et al. (2010) Evidence for multiple group 1 late embryogenesis abundant proteins in encysted embryos of artemia and their organelles. J. Biochem. 148, 581-92.
- Blouin C. M. et al. (2010) Lipid droplet analysis in caveolin-deficient adipocytes: Alterations in surface phospholipid composition and maturation defects. J. Lipid Res. 51, 945-56.
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