OPP (O-propargyl-puromycin)

OPP (O-propargyl-puromycin) is an alkyne analog of puromycin that is efficiently incorporated into newly translated proteins in complete methionine-containing media.

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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)
CAS#: 1416561-90-4
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

Applications:
Protein synthesis monitoring in cell culture and whole organisms[1,2]

Description:
Liu et al.[1] 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.[4] and Hong et al.[5] 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.

Selected References:
[1] 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.
[2] Signer et al. (2014) Haematopoietic stem cells require a highly regulated protein synthesis rate. Nature 509:49.
[3] Grammel et al. (2013) Chemical reporters for biological discovery. Nat. Chem. Biol. 9 (8):475.
[4] Presolski et al. (2011) Copper-Catalyzed Azide-Alkyne Click Chemistry for Bioconjugation. Current Protocols in Chemical Biology 3:153.
[5] Hong et al. (2011) Analysis and Optimization of Copper-Catalyzed Azide-Alkyne Cycloaddition for Bioconjugation. Angew. Chem. Int. Ed. 48:9879.