OPP (O-propargyl-puromycin) is an alkyne analog of puromycin that is efficiently incorporated into newly translated proteins in complete methionine-containing media.
For research use only!
Shipping: shipped on blue ice
Quantity: 3 mg
Storage Conditions: Store at -20 °C. One week to ambient temperature possible.
Shelf Life: 6 months after the date of delivery
Molecular Weight: 495.53 g/mol (free acid)
Purity: ≥ 95 % (HPLC)
Form: colorless to slightly white solid
Solubility: DMSO, PBS (up to 50 mM tested)
Spectroscopic Properties: λmax 275 nm; ε 20.0 L mmol-1 cm-1
Protein synthesis monitoring in cell culture and whole organisms[1,2]
Liu et al. reported a non-radioactive alternative to analyze newly synthesized proteins in cell culture and whole organisms that is based on O-Propargyl-puromycin, an alkyne analog of puromycin.
O-Propargyl-puromycin is cell-permeable and incorporates into the C-terminus of translating polypeptide chains thereby stopping translation.
The resulting truncated C-terminal alkyne labeled proteins can subsequently be detected via Cu(I)-catalyzed click chemistry that offers the choice to introduce a Biotin group (via Azides of Biotin) for subsequent purification tasks or a fluorescent group (via Azides of fluorescent dyes) for subsequent microscopic imaging.
In contrast to Azidohomoalanine (AHA) or Homopropargylgycine (HPG) based non-radioactive methionine analog-approaches, methionine free-medium is not required for O-Propargyl-purmoycin-based monitoring of nascent protein synthesis.
Presolski et al. and Hong et al. provide a general protocol for Cu(I)-catalyzed click chemistry reactions that may be used as a starting point for the set up and optimization of individual assays.
 Liu et al. (2012) Imaging protein synthesis in cells and tissues with an alkyne analog of puromycin. Proc. Natl. Acad. Sci. USA 109 (2):413.
 Signer et al. (2014) Haematopoietic stem cells require a highly regulated protein synthesis rate. Nature 509:49.
 Grammel et al. (2013) Chemical reporters for biological discovery. Nat. Chem. Biol. 9 (8):475.
 Presolski et al. (2011) Copper-Catalyzed Azide-Alkyne Click Chemistry for Bioconjugation. Current Protocols in Chemical Biology 3:153.
 Hong et al. (2011) Analysis and Optimization of Copper-Catalyzed Azide-Alkyne Cycloaddition for Bioconjugation. Angew. Chem. Int. Ed. 48:9879.