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Unnatural Azido Amino Acids for Monitoring Protein Synthesis
- Catalog No.
- 5.0 mg
- € 30,00
- 10 mg
- € 55,00
- 100 mg
- € 160,00
- 500 mg
- € 500,00
4-Azido-L-homoalanine hydrochloride can be incorporated into proteins by recombination methods to study and monitor protein synthesis.
Due to the azide-moiety, this molecule allows for specific bio-conjugation of various functionalities such as e.g. PEGs, antibodies or fluorescent labels, by click chemistry or Staudinger ligation. Therewith monitoring of protein synthesis can be performed.
Hong et al., Angew. Chemie Int. – Ed. 2011, 48, 9879
A Benitez-Mateos, I. Llarena, A. Sanchez-Iglesias, F. Lopez-Gallego, ACS Synthetic Biology, 2018, 7(3), 875-884.
Is it possible to generate azide- or alkyne-modified peptides or proteins?
Yes. Alkyne-modified peptides can be prepared by solid-phase synthesis. Please ask us directly, in case you are interested.
Due to technical reasons, preparation of azide-modified peptides by chemical synthesis is hardly possible.
How can de novo protein biosynthesis be monitored?
De novo protein biosynthesis can be monitored by feeding of metabolite analogues (so-called metabolic labeling) and subsequent click reaction. Azido-homoalanine for example is recognized as a methionine analogue and is incorporated into de novo synthesized proteins in methionine-free medium conditions. The resulting proteins contain azide moieties and thus can be detected after click to an alkyne-containing reporter molecule (e.g. a fluorescent dye). This non-radioactive method has major practical advantages compared to traditional 35S amino acid incorporation methods.
Alternatively, O-propargyl-puromycin is efficiently incorporated into proteins during de novo protein biosynthesis and can be used in complete medium. The resulting alkyne protein fragments can be detected via click to azide-containing reporter molecules.
What click conditions should be used for protein click reactions?
A catalyst system based on CuSO4 and sodium ascorbate is recommended in combination with Eterneon² dye azides to label alkyne-modified proteins. Please also refer to our general Click protocols for more details.
Due to the 20 (21) amino acids that are the building blocks of proteins, the physicochemical properties of proteins are more diverse compared to oligonucleotides, which are just composed of 5 major building blocks. Therefore, finding the optimal click conditions is more difficult compared to oligonucleotides and labeling rates are usually lower. Please note that despite these difficulties detection applications (e.g. de novo protein biosynthesis detection) are easily feasible.
- Is it possible to generate azide- or alkyne-modified peptides or proteins?
12 months unopened after receipt
2-8 °C, dry
144.13 g/mol * 36.45 g/mol
≥ 98% (HPLC)
white crystalline powder
942518-29-8 (hydrochloride salt)
120042-14-0 (free acid)
soluble in e.g. 0.1M NaOHaq
- Molecular Formula