Fluor-de-Lys^®-Propionyl substrate



BML-KI579-0050	50 µl	159.00 USD

Substrate provides a sensitive means to detect and quantify depropionylation activity with a variety of samples, including nuclear or cellular extracts, purified enzymes (HDACs and sirtuins), bead-bound immunocomplexes, etc. The Fluor de Lys^®-Propionyl Substrate, which comprises a propionylated lysine side chain, is first incubated with an active sample. Depropionylation of the substrate sensitizes the substrate so that, in a second step, treatment with the Fluor de Lys^® Developer produces a fluorophore (Ex. 360 nm; Em. 460 nm).

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Product Specification

Purity:	≥95% (HPLC)

Formulation:	50mM solution (50 μl) in dimethylsulfoxide (DMSO).

Long Term Storage:	-80°C

Miscellaneous/General:	Research demonstrates the occurrence of lysine post-translational acylations besides acetylation, including propionylation. Lysine propionylation has been observed in both eukaryotes and prokaryotes and on both histone and non-histone proteins. Acetyltransferases such as p300 and CBP have been found to catalyze propionylation and deacetylases, notably the sirtuins have been shown to have depropionylation activity.

Background / Technical Information:	Application: Study of HDAC or sirtuin kinetics, regulation and inhibitor sensitivity. Ideal for drug discovery and HTS applications. Notes: Must be used in conjunction with Fluor de Lys^® Developer (Prod. No. BML-KI105). For sirtuin assays, addition of the co-substrate NAD⁺ will be required. Assay fluorescence may be calibrated with the Fluor de Lys^® Deacetylated Standard (Prod. No. BML-KI142). For examples of appropriate assay conditions for class I or II HDACs see the Prod. No. BML-AK500 manual/protocol: For examples of appropriate assay conditions for sirtuins see the Prod. No. BML-AK555 manual/protocol:

General Literature References

Identification and characterization of propionylation at histone H3 lysine 23 in mammalian cells: B. Liu, et al.; J. Biol. Chem. 284, 32288 (2009), Abstract;

Identification and verification of lysine propionylation and butyrylation in yeast core histones using PTMap software: K. Zhang, et al.; J. Proteome Res. 8, 900 (2009), Abstract;

Molecular characterization of propionyllysines in non-histone proteins: Z. Cheng, et al.; Mol. Cell. Proteomics 8, 45 (2009), Abstract;

Acetyl-lysine analog peptides as mechanistic probes of protein deacetylases: B.C. Smith & J.M. Denu; J. Biol. Chem. 282, 37256 (2007), Abstract;

Lysine propionylation and butyrylation are novel post-translational modifications in histones: Y. Chen, et al.; Mol. Cell. Proteomics 6, 812 (2007), Abstract;

N-lysine propionylation controls the activity of propionyl-CoA synthetase: J. Garrity, et al.; J. Biol. Chem. 282, 30239 (2007), Abstract;