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 Teflon TFE-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
Trifluoroacetic Acid Specifications
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. Each lot of trifluoroacetic acid is tested to meet the following minimum specifications:
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
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 < 262 nm
Applications for Trifluoroacetic Acid
Ion pair reagent for reverse-phase HPLC1-3
Protein/peptide sequencing4-7
Protein/peptide solubilizing agent4-7
Solid-phase peptide synthesis8
Amino acid analysis
Making 0.1% solutions of trifluoroacetic acid (w/v vs. v/v)
References 1.Chicz, R.M. and Regnier, F.E. (1990) Methods Enzymol. 182, 392-421. 2.Zarember, K.A., et al. (2002) Infect. Immun. 70, 569-576. 3.Lassy, R.A. and Miller, C.G. (2000) J. Bacteriol. 182, 2536-2543. 4.Smith, B.J. (1997) Protein Sequencing Protocols. Humana Press. 5.Allen, G. (1989) Sequencing of Proteins and Peptides, Second Revised Addition. Elsevier. 6.Backstrom, J.R., et al. (1996) J. Neurosci. 16, 7910-7919. 7.Hermann, P.M., et al (2000) J. Neurosci. 20, 6355-6364. 8.Stuart, J.M. and Young, J.D. (1984) Solid Phase Peptide Synthesis, Second Edition. Pierce Chemical Company.