Palmitoylation is a post-translational modification (PTM) in which fatty acids, such as palmitic acid, are attached to an amino acid. These fatty acids are generally attached to the amino acid cysteine, however, can also be attached to serine and threonine. Palmitoylation plays a role in a protein's association with the cellular membrane because it enhances its hydrophobicity. Palmitoylation is reversible and the reverse reaction is catalyzed by palmitoyl protein thioesterases.
Palmitoylation Bioinformatics Tool
Laverne is a handy bioinformatics tool to help facilitate scientific exploration of related genes, diseases and pathways based on co-citations. Explore more on Palmitoylation below!
For more information on how to use Laverne, please read the How to Guide.
We have 534 products for the study of Palmitoylation that can be applied to Western Blot, Flow Cytometry, Immunocytochemistry/Immunofluorescence, Immunohistochemistry from our catalog of antibodies and ELISA kits.