S-Acylation (Commonly referred as S-palmitoylation)

Introduction

Protein S‑acylation is a reversible lipid modification involving the attachment of fatty acyl groups to cysteine residues through thioester bonds, with S‑palmitoylation being its predominant form. This dynamic modification regulates protein membrane association, trafficking, stability, and signaling, playing important roles in diverse cellular processes.

Products Solutions

Our human protein S‑acylation arrays combine selective labeling of S‑acylated cysteines with antibody‑based multiplex detection, enabling high‑throughput profiling of S‑acylation across hundreds to thousands of protein targets. Multiple array formats are available to support different screening scales and research needs.

• High‑throughput S‑acylation profiling
• Antibody‑based multiplex detection
• Broad protein target coverage
• Low sample input

Research Areas

• Cancer Research
• Neuroscience
• Immunology & Inflammation

References

1. Zhou L, Lian G, Zhou T, et al. Palmitoylation of GPX4 via the targetable ZDHHC8 determines ferroptosis sensitivity and antitumor immunity. Nat Cancer. 2025;6(5):768‑785.
2. Tong J, Liu Y, Wu W, et al. PPT1 selectively depalmitoylates GAP43 to regulate neuronal excitability and cognitive function. Sci Adv. 2026;12(20):eaeb4675.
3. Ni H, Wang Y, Yao K, et al. Cyclical palmitoylation regulates TLR9 signalling and systemic autoimmunity in mice. Nat Commun. 2024;15(1):1.