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).
Learn more about palmitoylation from our knowledge resource : https://badrilla.com/project-landing/
The Badrilla CAPTUREomeTM S-Palmitoylated protein kit is a simple and easy way of determining whether your protein of interest is post translationally modified with a palmitate group. The assay is based on the acyl-RAC (resin assisted capture) method and facilitates, with four simple steps – Block, Cleave, Capture and Analysis - determination of protein palmitoylation.
Kit highlights
The new CAPTUREomeTM S-Palmitoylation Mini Kit from Badrilla represents an affordable gateway into the emerging field of palmitoylation research. The Mini Kit, based on acyl RAC (resin assisted capture) technology, enables rapid determination of protein palmitoylation status from as little as 1mg of total cell lysate protein.
Badrilla’s Click S-Palmitoylation Detection775 KitTM provides a quick, convenient and robust method to identify S-palmitoylation of heterologously expressed proteins in cultured cells. The assay is based on the copper catalysed click chemistry reaction and facilitates, with four simple steps – Label, Lyse, Click and Detect - determination of protein palmitoylation.
Click S-Palmitoylation Detection775 Kit Enables
• Detection of S-palmitoylated proteins in cultured cells.
• Processing of 4 x 24 well cell culture plates (i.e. 96 samples in total).
• Convenient stopping point after labelling treatment.
Learn MoreHighly potent, selective inhibitor of APT1 (Acyl Palmitoyl Thio-esterase 1). 14 fold greater Selectivity for APT1 over APT2 and other serine hydrolases.
Learn MoreHighly potent, selective inhibitor of APT2 (Acyl Palmitoyl Thio-esterase 2).
Learn MoreThe 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.
Kit highlights
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
Kit highlights
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