Fig 2: Immunofluorescent-stained cryosections of mouse testis tissues using SCPX- and SCP2-specific antibodies.The analysis was performed to investigate the endogenous distribution of SCPX and SCP2 in the wild-type mouse testis. (A–B) SCPX is highly expressed in the interstitial connective tissue of the mouse testis, an area rich in Leydig cells, but is not expressed in the germ cells in the seminiferous tubules. (C–D) SCP2 was found to have the same distribution as SCPX, but with a lower level of expression. Scale bar, 50 µm.

Fig 3: Tumourigenicity in nude mice is inhibited by upregulated LINC00261. (A) Representative images of tumour xenografts and the tumour volume growth curve of nude mice. (B) Tumour weight in nude mice after treatment of oe-LINC00261. (C) Expression of VEGF in nude mice after treatment with oe-LINC00261, oe-FOXP3 or sh-SCP2 measured by IHC. (D) MVD in nude mice after treatment with oe-LINC00261, oe-FOXP3 or sh-SCP2 measured by IHC. (E and F) Expression of FOXP3, SCP2, Ki67, Cyclin D1, VEGF and Brachyury in nude mice after treatment with oe-LINC00261 or sh-LINC00261 measured by IHC and Western blot analysis. *p < 0.05 vs. the mice infected with blank vector. n = 5

Fig 4: Homology modelling of the mouse SCP2 domain and molecular docking studies of SCP2 with its potential ligands, cholesterol (Chol) and 22-NBD-cholesterol (22-NBD-Chol).(A–B) Molecular docking study using homology models based on the X-ray crystallography structure of the rabbit SCP2 (PBD: 1C44). (C–D) Molecular docking study using homology models based on the NMR structure of the human SCP2 (PBD: 1QND). (E–F) Molecular docking study using homology models based on the X-ray crystallography structure of the ligand-bound SCP2-like domain of human peroxisomal multifunctional enzyme type 2 (MFE-2; PDB: 1IKT). Cholesterol (Chol), 22-NBD-cholesterol (22-NBD-Chol), the Trp70 residue responsible for binding cholesterol, and the peroxisomal-targeting PTS1 signal (-AKL) are indicated. The calculated docking affinity (kcal/mol) from Autodock-Vina is indicated under each corresponding conformation.

Fig 5: Effects of DQP on blood free fatty acid and proteins of FAO pathway in heart tissue of HF rats after AMI. (A) Effects of DQP on blood free fatty acid. (B) WB bands of SCP2 and ACADL. (C) Protein quantitative results of SCP2 in heart tissues of rats. (D) Protein quantitative results of ACADL in heart tissues of rats. The raw date were listed in Supplementary Figure 1. ##P < 0.01 vs. sham group; **P < 0.01, ***P < 0.001 vs. model group.