Palmitoylation has emerged as an important post translational modification regulating protein function, intracellular trafficking and protein-protein as well as protein-lipid interactions. In particular it has generated much interest in the cardiovascular research community since it has been shown to regulate the function of key proteins that contribute to normal Ca2+ cycling and therefore myocyte contraction, as well as G-protein coupled receptors, important modulators of myocardial contractility.
Palmitoylation is the covalent attachment of a 16-carbon saturated fatty acid to a cysteine residue within a protein through the formation of a thioester or S-acyl bond. The process is mediated by a set of enzymes referred to as palmitoyl acyl transferases (PATs) together with the fatty acid donor palmitoyl CoA. There are 24 PAT enzymes which are characterised by a canonical zinc binding motif Asp-His-His-Cys (zDHHC). Furthermore, over 8000 palmitoylated proteins have been identified (a database of these proteins can be found at http://swisspalm.epfl.ch/ ). Palmitoylation can be constitutive in some instances, but can also be dynamic and reversible, in a manner analogous to phosphorylation – the palmitate group being removed by the activity of acyl palmitoyl thioesterases (APTs).
The new Badrilla SiteCounterTM S-Palmitoylated protein kit is a quick and easy way to quantify the extent of S-palmitoylation of your protein of interest. Using a straightforward mass tag approach, modification of each cysteine residue results in an incremental increase in the mass of the protein. The number of mobility shifts (as detected by western blot analysis) is observed as a ladder of protein bands, each ‘step’ in the ladder representing an additional s-palmitoylated cysteine residue.
The new Badrilla SiteCounterTM S-Palmitoylated Protein Mini Kit is a quick and easy way to quantify S-palmitoylation. Competitively priced, this starter kit provides a gateway into determining the number of palmitoylation sites in your protein of interest
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