Anti sdc1

Whole cell lysates were collected according to the manufacturer's instruction (Beyotime Biotechnology) and then centrifuged at 10,000 g for 10 min at 4°C. Then 1 mL supernatant was incubated with 1 μg anti-SDC1, anti-FLOT1, anti-Flag antibody (1:100, Proteintech Group), or anti-IgG antibody (1:100, Cell signaling Technology) for 16 h followed by addition of 20 μL protein A/G plus agarose beads (Santa Cruz Biotechnology) and incubated overnight at 4 °C. Protein samples were spun down, washed four times with immunoprecipitation buffer and heated for 10 min at 100 °C prior to loading on an SDS-PAGE gel for Western blot assay. Finally, the protein bands were visualized by ChemiDoc XRS system (Bio-Rad Laboratories Inc.). Antibodies are listed in supplementary Table S2.

Whole‐cell lysates were produced using a cell lysis solution from Cell Signalling Technology (Danvers, MA). The proteins were denatured by heating in loading buffer at 100°C for 10 min. Equal amounts of protein (50 μg) from all HGEC groups were separated using 8%–10% SDS‐PAGE and subsequently transferred onto PVDF membranes. These membranes were then blocked using a protein‐free rapid‐blocking solution (Beyotime Biotechnology, China) for 1 h. After the blocking step, the membranes underwent overnight incubation with designated primary antibodies at 4°C. The antibodies utilized in this investigation included anti‐β‐actin, anti‐HIC1, and anti‐Sirt7; anti‐SDC1, anti‐H3K18ac, anti‐CD31, anti‐αSMA, anti‐Snail, anti‐ERK1/2, and anti‐phospho‐ERK1/2 (ProteinTech, Wuhan, China). After undergoing five washes, the membranes were treated by secondary antibodies at ambient temperature for an hour, followed by another five washes with PBST. The protein signals were detected using an ECL system (Beyotime Institute of Biotechnology, Shanghai, China).