Thermo Scientific Pierce Fluoraldehyde Crystals are o-phthalaldehyde (OPA), a highly sensitive fluorescent derivatization reagent for peptide or amino acid detection and quantitation in HPLC.
Fluoraldehyde Crystals are a specially purified, fluorogenic-grade preparation of o-phthalaldehyde (OPA). This amine-reactive compound is primarily used for high-sensitivity, fluorescent detection of primary amines, including amino acids, peptides, proteins and polyamines in pre- or post-column chromatographic effluents.
Highlights:
- For pre- or post-column amino acid derivatization for fluorescent detection and quantitation
- Reacts with all primary amine-containing analytes to yield fluorescent derivatives (ex/em = 340nm/455nm)
- Provides an accurate measure of both composition and absolute protein-peptide content
- Ideal for work with recombinant proteins and synthetic peptides
- Can be used for fluorescent protein or peptide assay
- Can be prepared as a stable aqueous solution in borate (see instructions)
Reagent Properties:
- Alternative names: Fluoraldehyde Crystals, OPA
- Chemical name: ortho-Phthalaldehyde
- Reactive toward: Primary amines (–NH2)
- Chemical formula: C8H6O2
- CAS number: 643-79-8
- Molecular weight: 134.12
- Form: Pale yellow, free-flowing crystals
Product Details:
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Chemical structure of ortho-phthalaldehyde (OPA). Thermo Scientific Fluoraldehyde Crystals are high-purity crystalline OPA. For HPLC applications, OPA is usually used as reagent solution containing 2-mercaptoethanol. Consider using our ready-to-use Fluoraldehyde Reagent (Part No. 26025). |
For even greater sensitivity, use a combination of OPA and Fmoc-Chloride with automated pre-column derivatization to detect both primary and secondary amines. With this application, primary amino acids are first derivatized with OPA and then remaining secondary amino acids are reacted with Fmoc-Chloride, resulting in extraordinary amino acid detection sensitivity and accuracy (see Lindroth and Mopper, 1979; Lee and Drescher, 1979).
References:
- Lindroth, P. and Mopper, K. (1979). Anal. Chem. 51, 1667-1674.
- Lee, K.S. and Drescher, D.G. (1979). J. Biol. Chem. 254, 6248-6251.
- van Eijk, H.M.H., et al. (1988). Clin. Chem. 34, 2510-2513.
- Graser, T.A., et al. (1985). Anal. Biochem. 151, 142-152.
- Godel, H., et al. (1984). J. Chrom. 297, 49-61.
- Sista, H.S. (1986). J. Chrom. 359, 231-240.
- Cooper, J.D.H., et al. (1984). Anal. Biochem. 142, 98-102.
- Krishnamurti, C.R., et al. (1984). J. Chrom. 315, 321-331.
- Jones, B.N., et al. (1983). J. Chrom. 266, 471-482.
- Lee, H., et al. (1979). Anal. Biochem. 96, 298-307.
- Chen, R.F., et al. (1979). Biochem. Biophys. Acta. 576, 440-455.
- Jones, B.N., et al. (1981). J. Liq. Chrom. 4, 565-586.
- Benson, J.R. and Woo, D.J. (1984). J. Chromatogr. Sci. 22, 386-399.
- Krause, R.J., et al. (2002). Drug Metab. Dispos. 30, 1137.
- Atkinson, B.N., et al. (2001). Mol. Pharmacol. 60: 1414.
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