Sigma-Aldrich Alk-C16

Alkynyl palmitic acid (Alk-C16) is a modified palmitic acid consisting of a palmitic acid backbone with ω-terminal alkyne. This structure allows it to participate in bio-orthogonal reactions, particularly in copper-catalyzed click chemistry.

Alk-C16 is suitable for use as a palmitoylation probe in:

• fluorescence imaging to study palmitoylation dynamics during the cell cycle
• characterizing the mechanisms of pharmacological inhibitors of fatty acyltransferases
• biochemical and imaging detection of palmitoylated proteins in cells

Alk-C16 is useful for studying key signaling pathways such as Hedgehog and Wnt, which are known to involve palmitoylated proteins along with other proteins like α-tubulin, H-Ras, cGAS, p62, and TEAD. Additionally, Alk-C16 is widely employed in single-cell imaging and biochemical assays to detect S-palmitoylation and to explore lipid modifications in essential biological processes, including exosome production and protein homeostasis.

Bio-orthogonal probe used for metabolic labeling and fluorescence imaging of palmitoylated proteins.
Alkynyl Palmitic Acid (Alk-C16) is a bio-orthogonal probe designed for metabolic labeling of native palmitoylated proteins both in vitro and in vivo. It enables precise and chemoselective labeling via Cu(I)-catalyzed click chemistry, which involves the reaction of Alk-C16 with suitably tagged azides. This reaction allows for the efficient conjugation of fluorescent or biotinylated azides, facilitating high-resolution fluorescence imaging to reveal the subcellular localization of palmitoylated proteins and their association with cellular membranes. Alk-C16 specifically labels cysteine residues of palmitoylated proteins, making it particularly useful for studying dynamic palmitoylation and protein trafficking. Tools like Alk-C16 play a critical role in the identification and enrichment of lipidated proteins, advancing our ability to isolate and study palmitoylated proteins in complex biological systems.